692:
of models of chaperonin action have been proposed, which generally focus on two (not mutually exclusive) roles of chaperonin interior: passive and active. Passive models treat the chaperonin cage as an inert form, exerting influence by reducing the conformational space accessible to a protein substrate or preventing intermolecular interactions e.g. by aggregation prevention. The active chaperonin role is in turn involved with specific chaperonin–substrate interactions that may be coupled to conformational rearrangements of the chaperonin.
461:. The energy to fold proteins is supplied by non-covalent interactions between the amino acid side chains of each protein, and by solvent effects. Most proteins spontaneously fold into their most stable three-dimensional conformation, which is usually also their functional conformation, but occasionally proteins mis-fold. Molecular chaperones catalyze protein refolding by accelerating partial unfolding of misfolded proteins, aided by energy supplied by the hydrolysis of
593:
36:
495:
691:
The exact mechanism by which chaperonins facilitate folding of substrate proteins is unknown. According to recent analyses by different experimental techniques, GroEL-bound substrate proteins populate an ensemble of compact and locally expanded states that lack stable tertiary interactions. A number
687:
of ATP as well as binding of substrate proteins and cochaperonins, such as GroES. These conformational changes allow the chaperonin to bind an unfolded or misfolded protein, encapsulate that protein within one of the cavities formed by the two rings, and release the protein back into solution. Upon
473:
The structure of these chaperonins resemble two donuts stacked on top of one another to create a barrel. Each ring is composed of either 7, 8 or 9 subunits depending on the organism in which the chaperonin is found. Each ~60kDa peptide chain can be divided into three domains, apical, intermediate,
695:
Probably the most popular model of the chaperonin active role is the iterative annealing mechanism (IAM), which focuses on the effect of iterative, and hydrophobic in nature, binding of the protein substrate to the chaperonin. According to computational simulation studies, the IAM leads to more
655:
Group II chaperonins are not thought to utilize a GroES-type cofactor to fold their substrates. They instead contain a "built-in" lid that closes in an ATP-dependent manner to encapsulate its substrates, a process that is required for optimal protein folding activity. They also interact with a
1920:
Snustad DP (August 1968). "Dominance interactions in
Escherichia coli cells mixedly infected with bacteriophage T4D wild-type and amber mutants and their possible implications as to type of gene-product function: catalytic vs. stoichiometric".
445:
originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called
563:
The Cpn60 subfamily was discovered in 1988. It was sequenced in 1992. The cpn10 and cpn60 oligomers also require Mg-ATP in order to interact to form a functional complex. The binding of cpn10 to cpn60 inhibits the weak
817:, a source of oxygen radicals. Cpn60 has also been found to display strong antigenicity in many bacterial species and has the potential for inducing immune protection against unrelated bacterial infections.
652:
chaperonin (Mm cpn) is composed of sixteen identical subunits (eight per ring). It has been shown to fold the mitochondrial protein rhodanese; however, no natural substrates have yet been identified.
643:, each thought to be represented once per eight-membered ring. TRiC was originally thought to fold only the cytoskeletal proteins actin and tubulin but is now known to fold dozens of substrates.
793:
The main reason for the phage to need its own GroES homolog is that the gp23 protein is too large to fit into a conventional GroES cage. gp31 has longer loops that create a taller container.
668:
Group III includes some bacterial Cpns that are related to Group II. They have a lid, but the lid opening is noncooperative in them. They are thought to be an ancient relative of Group II.
1266:
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, et al. (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly".
1317:
Prasad TK, Stewart CR (March 1992). "cDNA clones encoding
Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock".
1504:
Zang Y, Jin M, Wang H, Cui Z, Kong L, Liu C, Cong Y (December 2016). "Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM".
2143:
2080:
560:
GroEL/GroES may not be able to undo protein aggregates, but kinetically it competes in the pathway of misfolding and aggregation, thereby preventing aggregate formation.
171:
1453:
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A".
975:
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A".
2216:
3020:
1170:
Willison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring".
2116:
754:
and higher eukaryotes. While there are differences between eukaryotic, bacterial and archaeal chaperonins, the general structure and mechanism are conserved.
2469:
696:
productive folding by unfolding the substrate from misfolded conformations or by prevention from protein misfolding through changing the folding pathway.
688:
release, the substrate protein will either be folded or will require further rounds of folding, in which case it can again be bound by a chaperonin.
2151:
900:
2879:
2209:
890:
672:
2107:
881:
782:
and is able to substitute for it in the assembly of phage T4 virions during infection. Like GroES, gp31 forms a stable complex with
2124:
2768:
2763:
2738:
2728:
2723:
2713:
886:
2784:
2718:
2202:
871:
675:
does not use a lid, and its donut interface is more similar to Group II. It might represent another ancient type of chaperonin.
3015:
2814:
834:
1026:
2077:
941:
The GroEL family is referred to, by InterPro, as Cpn60. However, CDD uses Cpn60 to refer to the Group II proteins in archaea.
107:
191:
3032:
1549:"Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis"
2225:
1762:"Simulation of chaperonin effect on protein folding: a shift from nucleation-condensation to framework mechanism"
3062:
2425:
179:
3067:
1863:"Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism"
3057:
2638:
2039:
Gor D, Mayfield JE (February 1992). "Cloning and nucleotide sequence of the
Brucella abortus groE operon".
1960:
2160:
774:
is the host for bacteriophage T4. The bacteriophage encoded gp31 protein appears to be homologous to the
683:
Chaperonins undergo large conformational changes during a folding reaction as a function of the enzymatic
2583:
1362:"Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis"
1223:
Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide".
458:
175:
2170:
648:
127:
120:
2148:
1655:
Hartl FU, Hayer-Hartl M (June 2009). "Converging concepts of protein folding in vitro and in vivo".
132:
3072:
2523:
2174:
2093:
750:
2848:
1700:"Chaperonin chamber accelerates protein folding through passive action of preventing aggregation"
2889:
954:
is known to have five types of subunits. The ancestor to eukarotic TriC is thought to have two.
462:
1030:
2270:
813:. This hypothesis is based on the finding that the cpn60 gene is upregulated in response to
542:
patch at its opening and can accommodate the native folding of substrates 15-60 kDa in size.
2104:
1874:
1711:
1609:
1462:
1275:
984:
763:
447:
158:
2165:
2133:
8:
2233:
2121:
1809:
Chakraborty K, Chatila M, Sinha J, Shi Q, Poschner BC, Sikor M, et al. (July 2010).
912:
806:
805:, and is thought to play a role in the protection of the Legionella bacteria from oxygen
442:
1878:
1715:
1613:
1466:
1279:
988:
531:
is a Group I chaperonin and the best characterized large (~ 1 MDa) chaperonin complex.
2247:
2089:
2021:
1840:
1786:
1761:
1734:
1699:
1680:
1632:
1597:
1573:
1548:
1529:
1486:
1430:
1413:
1342:
1299:
1248:
1205:
1144:
1117:
1088:
1063:
1008:
917:
584:
Some bacteria use multiple copies of this chaperonin, probably for different peptides.
2008:
1991:
1386:
1361:
633:. A homo-16mer in some archaea, it is regarded as the prototypical type II chaperonin.
2549:
2056:
2052:
2013:
1972:
1938:
1934:
1902:
1897:
1862:
1832:
1791:
1739:
1684:
1672:
1637:
1578:
1521:
1478:
1435:
1391:
1377:
1334:
1291:
1240:
1197:
1149:
1093:
1000:
922:
814:
602:
198:
166:
112:
2025:
1596:
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 April 2020).
1533:
1346:
1252:
1209:
64:
2809:
2513:
2048:
2003:
1930:
1892:
1882:
1844:
1822:
1781:
1773:
1729:
1719:
1664:
1627:
1617:
1568:
1560:
1513:
1490:
1470:
1425:
1381:
1373:
1326:
1303:
1283:
1232:
1187:
1179:
1139:
1129:
1083:
1075:
1012:
992:
577:
549:
154:
19:
This article is about the protein family. For the human mitochondrial protein, see
2138:
2238:
2194:
2190:
2155:
2128:
2111:
2084:
1622:
454:
76:
639:, the eukaryotic chaperonin, is composed of two rings of eight different though
2562:
2557:
1867:
Proceedings of the
National Academy of Sciences of the United States of America
1827:
1810:
1704:
Proceedings of the
National Academy of Sciences of the United States of America
770:
rather than being incorporated into the bacteriophage structure. The bacterium
737:
636:
1811:"Chaperonin-catalyzed rescue of kinetically trapped states in protein folding"
1236:
1079:
3051:
1134:
802:
575:
subunit binding protein is a member of this family. The crystal structure of
511:
478:
95:
1724:
465:(ATP). Chaperonin proteins may also tag misfolded proteins to be degraded.
2918:
2900:
1887:
1836:
1795:
1743:
1676:
1641:
1582:
1525:
1244:
1201:
1192:
1153:
1097:
519:
515:
2060:
2017:
1976:
1942:
1906:
1598:"Structure and conformational cycle of a bacteriophage-encoded chaperonin"
1482:
1439:
1395:
1338:
1295:
1118:"A Glimpse Into the Structure and Function of Atypical Type I Chaperonins"
1004:
116:
2994:
2862:
950:
Some archaeons have evolved to use, like eukaryotes, different subunits.
850:
838:
548:(is a single-ring heptamer that binds to GroEL in the presence of ATP or
539:
1183:
592:
2824:
1564:
1330:
810:
726:
684:
630:
615:
507:
88:
1777:
1668:
1517:
1360:
Schmidt A, Schiesswohl M, Völker U, Hecker M, Schumann W (June 1992).
606:
2572:
2518:
1474:
1287:
996:
786:
chaperonin that is absolutely necessary for the folding and assembly
767:
699:
657:
416:
410:
404:
397:
391:
385:
379:
373:
367:
361:
355:
349:
343:
337:
331:
325:
319:
313:
307:
301:
295:
289:
283:
277:
271:
265:
259:
253:
247:
241:
235:
229:
223:
216:
210:
204:
2852:
2485:
2477:
2186:
2041:
Biochimica et
Biophysica Acta (BBA) - Gene Structure and Expression
1265:
503:
71:
100:
2603:
2490:
2450:
2381:
2376:
2371:
2366:
2361:
2316:
1061:
733:
722:
714:
640:
622:
618:
572:
527:
83:
1062:
Conway de
Macario E, Yohda M, Macario AJ, Robb FT (2019-03-15).
766:
is a protein required for bacteriophage morphogenesis that acts
708:
In bacteria, the archetype is the well-characterized chaperonin
2819:
2794:
2789:
2779:
2743:
2733:
2708:
2693:
2688:
2683:
2678:
2673:
2668:
2663:
2658:
2623:
2608:
2455:
2420:
2405:
2400:
2395:
2356:
2351:
2346:
2341:
2336:
2331:
2326:
2321:
2311:
2306:
2301:
2296:
2291:
1497:
565:
186:
35:
1958:
1359:
825:
Human genes encoding proteins containing this domain include:
494:
3010:
3000:
2990:
2975:
2957:
2952:
2947:
2942:
2874:
2834:
2799:
2773:
2758:
2753:
2748:
2703:
2698:
2653:
2648:
2643:
2613:
2598:
2495:
2464:
2445:
2440:
2435:
2430:
2415:
2410:
2390:
2286:
2279:
2275:
2265:
2260:
876:
858:
854:
829:
783:
779:
709:
545:
535:
20:
1452:
1414:"Sequence analysis of the Legionella micdadei groELS operon"
974:
457:
from a linear chain of amino acids into a three-dimensional
3025:
3005:
2985:
2980:
2930:
2913:
2869:
2857:
2839:
2829:
2628:
2618:
2593:
2588:
2533:
2528:
2182:
1064:"Bridging human chaperonopathies and microbial chaperonins"
895:
866:
862:
846:
842:
801:
Human GroEL is the immunodominant antigen of patients with
744:
These protein complexes appear to be essential for life in
477:
The original chaperonin is proposed to have evolved from a
148:
59:
1959:
Marusich EI, Kurochkina LP, Mesyanzhinov VV (April 1998).
1808:
1595:
1512:(12). Springer Science and Business Media LLC: 1083–1091.
1411:
736:, the cytoplasmic chaperonin is called CCT (also called
2181:
This article incorporates text from the public domain
2099:
1802:
1755:
1753:
1027:"Howard Hughes Investigators: Arthur L. Horwich, M.D."
1860:
1648:
556:. It is like a cover that covers GroEL (box/bottle).
1750:
1412:Hindersson P, Høiby N, Bangsborg J (January 1991).
790:of the bacteriophage T4 major capsid protein gp23.
2224:
1856:
1854:
700:Conservation of structural and functional homology
1691:
1546:
757:
3049:
1861:Todd MJ, Lorimer GH, Thirumalai D (April 1996).
1654:
1954:
1952:
1851:
1759:
1503:
1407:
1405:
1111:
1109:
1107:
704:As mentioned, all cells contain chaperonins.
2210:
1697:
1540:
1316:
1222:
1989:
1949:
1913:
552:analogues of ATP hydrolysis, such as ADP-AlF
40:Structure of the bacterial chaperonin GroEL.
2038:
2032:
1446:
1402:
1353:
1216:
1115:
1104:
614:Group II chaperonins (TCP-1), found in the
2217:
2203:
1310:
1259:
1165:
1163:
968:
34:
2173:at the U.S. National Library of Medicine
2092:at the U.S. National Library of Medicine
2007:
1961:"Chaperones in bacteriophage T4 assembly"
1896:
1886:
1826:
1785:
1733:
1723:
1657:Nature Structural & Molecular Biology
1631:
1621:
1572:
1506:Nature Structural & Molecular Biology
1429:
1385:
1191:
1143:
1133:
1087:
502:Group I chaperonins (Cpn60) are found in
1992:"The Hsp70 and Hsp60 chaperone machines"
1766:Journal of the American Chemical Society
1169:
796:
591:
493:
1919:
1698:Apetri AC, Horwich AL (November 2008).
1160:
3050:
678:
2198:
2105:Animations of activity of Chaperonins
1990:Bukau B, Horwich AL (February 1998).
1547:Kusmierczyk AR, Martin J (May 2003).
629:The complex in archaea is called the
538:is a double-ring 14mer with a greasy
1057:
1055:
1053:
1051:
1049:
1047:
660:, that helps move the substrate in.
1760:Kmiecik S, Kolinski A (July 2011).
13:
3033:Prokaryotic ubiquitin-like protein
1431:10.1111/j.1574-6968.1991.tb04317.x
1122:Frontiers in Molecular Biosciences
581:GroEL has been resolved to 2.8 Ă….
14:
3084:
2071:
1044:
663:
625:, are more poorly characterized.
600:TRiC in the AMP-PNP bound state (
484:
453:Newly made proteins usually must
1378:10.1128/jb.174.12.3993-3999.1992
671:A Group I chaperonin gp146 from
1983:
1589:
1225:Quarterly Reviews of Biophysics
944:
725:, the chaperonin is called the
2563:Mitochondrial targeting signal
2226:Posttranslational modification
1019:
935:
762:The gene product 31 (gp31) of
758:Bacteriophage T4 morphogenesis
1:
2009:10.1016/S0092-8674(00)80928-9
961:
143:Available protein structures:
29:TCP-1/cpn60 chaperonin family
2639:Ubiquitin-conjugating enzyme
2100:cpnDB: a chaperonin database
2053:10.1016/0167-4781(92)90476-g
1935:10.1016/0042-6822(68)90285-7
1623:10.1371/journal.pone.0230090
1116:Ansari MY, Mande SC (2018).
468:
7:
2927:E2 SUMO-conjugating enzyme
2584:Ubiquitin-activating enzyme
906:
820:
587:
525:The GroEL/GroES complex in
10:
3089:
2910:E1 SUMO-activating enzyme
2180:
1828:10.1016/j.cell.2010.05.027
952:Methanosarcina acetivorans
498:GroES/GroEL complex (side)
489:
18:
2968:
2899:
2888:
2571:
2548:
2506:
2246:
2232:
2171:HSP60+Heat-Shock+Proteins
1418:FEMS Microbiology Letters
1237:10.1017/S0033583503003883
1080:10.1038/s42003-019-0318-5
649:Methanococcus maripaludis
197:
185:
165:
147:
142:
138:
126:
106:
94:
82:
70:
58:
50:
45:
33:
28:
2524:Survival of motor neuron
2175:Medical Subject Headings
2149:Enzyme Database on HSP60
2139:The Chaperonin Home Page
2094:Medical Subject Headings
1135:10.3389/fmolb.2018.00031
928:
751:Saccharomyces cerevisiae
598:Saccharomyces cerevisiae
2890:Ubiquitin-like proteins
2849:Deubiquitinating enzyme
1725:10.1073/pnas.0809794105
1553:The Biochemical Journal
1366:Journal of Bacteriology
1319:Plant Molecular Biology
1172:The Biochemical Journal
1888:10.1073/pnas.93.9.4030
1068:Communications Biology
611:
499:
463:adenosine triphosphate
3063:Moonlighting proteins
2144:The Protein Data Bank
2117:NIH Material on HSP60
1965:Biochemistry (Moscow)
803:Legionnaire's disease
797:Clinical significance
778:cochaperonin protein
595:
497:
3068:Molecular chaperones
448:molecular chaperones
3058:Heat shock proteins
2248:Heat shock proteins
1879:1996PNAS...93.4030T
1716:2008PNAS..10517351A
1614:2020PLoSO..1530090B
1467:1994Natur.371..578B
1280:1988Natur.333..330H
1184:10.1042/BCJ20170378
989:1994Natur.371..578B
679:Mechanism of action
568:activity of cpn60.
443:heat shock proteins
2154:2021-04-18 at the
2127:2008-03-16 at the
2110:2021-04-13 at the
2083:2011-03-01 at the
1565:10.1042/BJ20030230
1331:10.1007/BF00019202
918:Heat shock protein
612:
500:
459:tertiary structure
441:), is a family of
3045:
3044:
3041:
3040:
2550:Protein targeting
2544:
2543:
2166:HSP60 Gene Report
1778:10.1021/ja203275f
1669:10.1038/nsmb.1591
1518:10.1038/nsmb.3309
1178:(19): 3009–3034.
923:Arthur L. Horwich
815:hydrogen peroxide
428:
427:
424:
423:
192:structure summary
3080:
2897:
2896:
2810:Ubiquitin ligase
2576:(ubiquitylation)
2514:Alpha crystallin
2244:
2243:
2219:
2212:
2205:
2196:
2195:
2161:HSP60 on Pub Med
2065:
2064:
2036:
2030:
2029:
2011:
1987:
1981:
1980:
1956:
1947:
1946:
1917:
1911:
1910:
1900:
1890:
1858:
1849:
1848:
1830:
1806:
1800:
1799:
1789:
1757:
1748:
1747:
1737:
1727:
1695:
1689:
1688:
1652:
1646:
1645:
1635:
1625:
1593:
1587:
1586:
1576:
1559:(Pt 3): 669–73.
1544:
1538:
1537:
1501:
1495:
1494:
1475:10.1038/371578a0
1461:(6498): 578–86.
1450:
1444:
1443:
1433:
1409:
1400:
1399:
1389:
1357:
1351:
1350:
1314:
1308:
1307:
1288:10.1038/333330a0
1263:
1257:
1256:
1220:
1214:
1213:
1195:
1167:
1158:
1157:
1147:
1137:
1113:
1102:
1101:
1091:
1059:
1042:
1041:
1039:
1038:
1023:
1017:
1016:
997:10.1038/371578a0
983:(6498): 578–86.
972:
955:
948:
942:
939:
764:bacteriophage T4
641:related subunits
609:
578:Escherichia coli
550:transition state
474:and equatorial.
433:, also known as
419:
413:
407:
400:
394:
388:
382:
376:
370:
364:
358:
352:
346:
340:
334:
328:
322:
316:
310:
304:
298:
292:
286:
280:
274:
268:
262:
256:
250:
244:
238:
232:
226:
219:
213:
207:
140:
139:
38:
26:
25:
3088:
3087:
3083:
3082:
3081:
3079:
3078:
3077:
3073:Protein folding
3048:
3047:
3046:
3037:
2964:
2939:E3 SUMO ligase
2903:
2892:
2884:
2575:
2567:
2540:
2502:
2481:
2473:
2251:
2239:protein folding
2237:
2228:
2223:
2193:
2156:Wayback Machine
2129:Wayback Machine
2112:Wayback Machine
2085:Wayback Machine
2078:more details...
2074:
2069:
2068:
2037:
2033:
1988:
1984:
1957:
1950:
1918:
1914:
1859:
1852:
1807:
1803:
1772:(26): 10283–9.
1758:
1751:
1710:(45): 17351–5.
1696:
1692:
1653:
1649:
1608:(4): e0230090.
1594:
1590:
1545:
1541:
1502:
1498:
1451:
1447:
1410:
1403:
1358:
1354:
1315:
1311:
1274:(6171): 330–4.
1264:
1260:
1221:
1217:
1168:
1161:
1114:
1105:
1060:
1045:
1036:
1034:
1025:
1024:
1020:
973:
969:
964:
959:
958:
949:
945:
940:
936:
931:
909:
823:
799:
760:
702:
681:
666:
601:
590:
555:
492:
487:
471:
415:
409:
403:
396:
390:
384:
378:
372:
366:
360:
354:
348:
342:
336:
330:
324:
318:
312:
306:
300:
294:
288:
282:
276:
270:
264:
258:
252:
246:
240:
234:
228:
222:
215:
209:
203:
41:
24:
17:
16:InterPro Family
12:
11:
5:
3086:
3076:
3075:
3070:
3065:
3060:
3043:
3042:
3039:
3038:
3036:
3035:
3029:
3028:
3023:
3018:
3013:
3008:
3003:
2998:
2988:
2983:
2978:
2972:
2970:
2966:
2965:
2963:
2962:
2961:
2960:
2955:
2950:
2945:
2936:
2935:
2934:
2933:
2924:
2923:
2922:
2921:
2916:
2907:
2905:
2894:
2886:
2885:
2883:
2882:
2877:
2872:
2866:
2865:
2860:
2855:
2845:
2844:
2843:
2842:
2837:
2832:
2827:
2822:
2817:
2805:
2804:
2803:
2802:
2797:
2792:
2787:
2782:
2777:
2771:
2766:
2761:
2756:
2751:
2746:
2741:
2736:
2731:
2726:
2721:
2716:
2711:
2706:
2701:
2696:
2691:
2686:
2681:
2676:
2671:
2666:
2661:
2656:
2651:
2646:
2634:
2633:
2632:
2631:
2626:
2621:
2616:
2611:
2606:
2601:
2596:
2591:
2579:
2577:
2569:
2568:
2566:
2565:
2560:
2558:Signal peptide
2554:
2552:
2546:
2545:
2542:
2541:
2539:
2538:
2537:
2536:
2531:
2521:
2516:
2510:
2508:
2504:
2503:
2501:
2500:
2499:
2498:
2493:
2488:
2483:
2479:
2475:
2471:
2461:
2460:
2459:
2458:
2453:
2448:
2443:
2438:
2433:
2428:
2423:
2418:
2413:
2408:
2403:
2398:
2387:
2386:
2385:
2384:
2379:
2374:
2369:
2364:
2359:
2354:
2349:
2344:
2339:
2334:
2329:
2324:
2319:
2314:
2309:
2304:
2299:
2294:
2283:
2282:
2273:
2268:
2263:
2257:
2255:
2241:
2230:
2229:
2222:
2221:
2214:
2207:
2199:
2179:
2178:
2168:
2163:
2158:
2146:
2141:
2136:
2134:HSP60 in Flies
2131:
2119:
2114:
2102:
2097:
2087:
2073:
2072:External links
2070:
2067:
2066:
2031:
1982:
1971:(4): 399–406.
1948:
1912:
1850:
1801:
1749:
1690:
1647:
1588:
1539:
1496:
1445:
1401:
1372:(12): 3993–9.
1352:
1309:
1258:
1215:
1159:
1103:
1043:
1029:Archived from
1018:
966:
965:
963:
960:
957:
956:
943:
933:
932:
930:
927:
926:
925:
920:
915:
908:
905:
904:
903:
898:
893:
884:
879:
874:
869:
832:
822:
819:
798:
795:
759:
756:
742:
741:
730:
719:
701:
698:
680:
677:
665:
664:Other families
662:
656:co-chaperone,
645:
644:
634:
589:
586:
558:
557:
553:
543:
491:
488:
486:
485:Classification
483:
470:
467:
426:
425:
422:
421:
201:
195:
194:
189:
183:
182:
169:
163:
162:
152:
145:
144:
136:
135:
130:
124:
123:
110:
104:
103:
98:
92:
91:
86:
80:
79:
74:
68:
67:
62:
56:
55:
52:
48:
47:
43:
42:
39:
31:
30:
15:
9:
6:
4:
3:
2:
3085:
3074:
3071:
3069:
3066:
3064:
3061:
3059:
3056:
3055:
3053:
3034:
3031:
3030:
3027:
3024:
3022:
3019:
3017:
3014:
3012:
3009:
3007:
3004:
3002:
2999:
2996:
2992:
2989:
2987:
2984:
2982:
2979:
2977:
2974:
2973:
2971:
2967:
2959:
2956:
2954:
2951:
2949:
2946:
2944:
2941:
2940:
2938:
2937:
2932:
2929:
2928:
2926:
2925:
2920:
2917:
2915:
2912:
2911:
2909:
2908:
2906:
2904:(SUMOylation)
2902:
2898:
2895:
2891:
2887:
2881:
2878:
2876:
2873:
2871:
2868:
2867:
2864:
2861:
2859:
2856:
2854:
2850:
2847:
2846:
2841:
2838:
2836:
2833:
2831:
2828:
2826:
2823:
2821:
2818:
2816:
2813:
2812:
2811:
2807:
2806:
2801:
2798:
2796:
2793:
2791:
2788:
2786:
2783:
2781:
2778:
2775:
2772:
2770:
2767:
2765:
2762:
2760:
2757:
2755:
2752:
2750:
2747:
2745:
2742:
2740:
2737:
2735:
2732:
2730:
2727:
2725:
2722:
2720:
2717:
2715:
2712:
2710:
2707:
2705:
2702:
2700:
2697:
2695:
2692:
2690:
2687:
2685:
2682:
2680:
2677:
2675:
2672:
2670:
2667:
2665:
2662:
2660:
2657:
2655:
2652:
2650:
2647:
2645:
2642:
2641:
2640:
2636:
2635:
2630:
2627:
2625:
2622:
2620:
2617:
2615:
2612:
2610:
2607:
2605:
2602:
2600:
2597:
2595:
2592:
2590:
2587:
2586:
2585:
2581:
2580:
2578:
2574:
2570:
2564:
2561:
2559:
2556:
2555:
2553:
2551:
2547:
2535:
2532:
2530:
2527:
2526:
2525:
2522:
2520:
2517:
2515:
2512:
2511:
2509:
2505:
2497:
2494:
2492:
2489:
2487:
2484:
2482:
2476:
2474:
2468:
2467:
2466:
2463:
2462:
2457:
2454:
2452:
2449:
2447:
2444:
2442:
2439:
2437:
2434:
2432:
2429:
2427:
2424:
2422:
2419:
2417:
2414:
2412:
2409:
2407:
2404:
2402:
2399:
2397:
2394:
2393:
2392:
2389:
2388:
2383:
2380:
2378:
2375:
2373:
2370:
2368:
2365:
2363:
2360:
2358:
2355:
2353:
2350:
2348:
2345:
2343:
2340:
2338:
2335:
2333:
2330:
2328:
2325:
2323:
2320:
2318:
2315:
2313:
2310:
2308:
2305:
2303:
2300:
2298:
2295:
2293:
2290:
2289:
2288:
2285:
2284:
2281:
2277:
2274:
2272:
2269:
2267:
2264:
2262:
2259:
2258:
2256:
2254:
2249:
2245:
2242:
2240:
2235:
2231:
2227:
2220:
2215:
2213:
2208:
2206:
2201:
2200:
2197:
2192:
2188:
2184:
2176:
2172:
2169:
2167:
2164:
2162:
2159:
2157:
2153:
2150:
2147:
2145:
2142:
2140:
2137:
2135:
2132:
2130:
2126:
2123:
2120:
2118:
2115:
2113:
2109:
2106:
2103:
2101:
2098:
2095:
2091:
2088:
2086:
2082:
2079:
2076:
2075:
2062:
2058:
2054:
2050:
2046:
2042:
2035:
2027:
2023:
2019:
2015:
2010:
2005:
2002:(3): 351–66.
2001:
1997:
1993:
1986:
1978:
1974:
1970:
1966:
1962:
1955:
1953:
1944:
1940:
1936:
1932:
1929:(4): 550–63.
1928:
1924:
1916:
1908:
1904:
1899:
1894:
1889:
1884:
1880:
1876:
1873:(9): 4030–5.
1872:
1868:
1864:
1857:
1855:
1846:
1842:
1838:
1834:
1829:
1824:
1821:(1): 112–22.
1820:
1816:
1812:
1805:
1797:
1793:
1788:
1783:
1779:
1775:
1771:
1767:
1763:
1756:
1754:
1745:
1741:
1736:
1731:
1726:
1721:
1717:
1713:
1709:
1705:
1701:
1694:
1686:
1682:
1678:
1674:
1670:
1666:
1663:(6): 574–81.
1662:
1658:
1651:
1643:
1639:
1634:
1629:
1624:
1619:
1615:
1611:
1607:
1603:
1599:
1592:
1584:
1580:
1575:
1570:
1566:
1562:
1558:
1554:
1550:
1543:
1535:
1531:
1527:
1523:
1519:
1515:
1511:
1507:
1500:
1492:
1488:
1484:
1480:
1476:
1472:
1468:
1464:
1460:
1456:
1449:
1441:
1437:
1432:
1427:
1423:
1419:
1415:
1408:
1406:
1397:
1393:
1388:
1383:
1379:
1375:
1371:
1367:
1363:
1356:
1348:
1344:
1340:
1336:
1332:
1328:
1325:(5): 873–85.
1324:
1320:
1313:
1305:
1301:
1297:
1293:
1289:
1285:
1281:
1277:
1273:
1269:
1262:
1254:
1250:
1246:
1242:
1238:
1234:
1231:(2): 229–56.
1230:
1226:
1219:
1211:
1207:
1203:
1199:
1194:
1193:10044/1/63924
1189:
1185:
1181:
1177:
1173:
1166:
1164:
1155:
1151:
1146:
1141:
1136:
1131:
1127:
1123:
1119:
1112:
1110:
1108:
1099:
1095:
1090:
1085:
1081:
1077:
1073:
1069:
1065:
1058:
1056:
1054:
1052:
1050:
1048:
1033:on 2019-07-26
1032:
1028:
1022:
1014:
1010:
1006:
1002:
998:
994:
990:
986:
982:
978:
971:
967:
953:
947:
938:
934:
924:
921:
919:
916:
914:
911:
910:
902:
899:
897:
894:
892:
888:
885:
883:
880:
878:
875:
873:
870:
868:
864:
860:
856:
852:
848:
844:
840:
836:
833:
831:
828:
827:
826:
818:
816:
812:
808:
804:
794:
791:
789:
785:
781:
777:
773:
769:
768:catalytically
765:
755:
753:
752:
747:
739:
735:
731:
728:
724:
720:
717:
716:
711:
707:
706:
705:
697:
693:
689:
686:
676:
674:
669:
661:
659:
653:
651:
650:
642:
638:
635:
632:
628:
627:
626:
624:
620:
617:
608:
604:
599:
596:Structure of
594:
585:
582:
580:
579:
574:
569:
567:
561:
551:
547:
544:
541:
537:
534:
533:
532:
530:
529:
523:
521:
517:
513:
512:endosymbiotic
509:
505:
496:
482:
480:
479:peroxiredoxin
475:
466:
464:
460:
456:
451:
449:
444:
440:
436:
432:
418:
412:
406:
402:
399:
393:
387:
383:B:33-521
381:
375:
369:
365:E:22-526
363:
357:
351:
347:A:187-378
345:
339:
333:
329:A:190-375
327:
321:
315:
309:
303:
297:
293:H:23-525
291:
285:
279:
275:C:190-335
273:
267:
261:
257:I:23-525
255:
249:
243:
239:E:23-525
237:
231:
225:
220:A:190-375
218:
212:
206:
202:
200:
196:
193:
190:
188:
184:
181:
177:
173:
170:
168:
164:
160:
156:
153:
150:
146:
141:
137:
134:
131:
129:
125:
122:
118:
114:
111:
109:
105:
102:
99:
97:
93:
90:
87:
85:
81:
78:
75:
73:
69:
66:
63:
61:
57:
53:
49:
44:
37:
32:
27:
22:
2901:SUMO protein
2252:
2047:(1): 120–2.
2044:
2040:
2034:
1999:
1995:
1985:
1968:
1964:
1926:
1922:
1915:
1870:
1866:
1818:
1814:
1804:
1769:
1765:
1707:
1703:
1693:
1660:
1656:
1650:
1605:
1601:
1591:
1556:
1552:
1542:
1509:
1505:
1499:
1458:
1454:
1448:
1421:
1417:
1369:
1365:
1355:
1322:
1318:
1312:
1271:
1267:
1261:
1228:
1224:
1218:
1175:
1171:
1125:
1121:
1071:
1067:
1035:. Retrieved
1031:the original
1021:
980:
976:
970:
951:
946:
937:
824:
800:
792:
787:
775:
771:
761:
749:
745:
743:
713:
703:
694:
690:
682:
670:
667:
654:
647:
646:
613:
597:
583:
576:
570:
562:
559:
526:
524:
520:mitochondria
516:chloroplasts
501:
476:
472:
452:
438:
434:
430:
429:
414:H:210-380
401::214-364
395:B:215-366
389:B:33-521
377:A:1-143
371:B:42-522
359:e:22-526
353:A:23-526
335:A:190-335
323:B:23-524
317:F:23-525
311::190-375
305:E:23-524
299:H:23-525
287:E:23-524
281:L:23-525
269:K:23-525
263:J:23-524
251:J:23-524
245:J:23-524
233:F:23-525
227:H:23-525
221:
214:Z:23-525
208:K:23-525
2995:neddylation
2261:Hsp10/GroES
2253:Chaperonins
2090:Chaperonins
1424:(1): 31–8.
811:macrophages
540:hydrophobic
506:as well as
435:chaperonins
408::214-364
341::190-335
46:Identifiers
3052:Categories
2287:Hsp40/DnaJ
2234:Chaperones
1074:(1): 103.
1037:2011-09-12
962:References
727:thermosome
685:hydrolysis
631:thermosome
616:eukaryotic
508:organelles
155:structures
54:Cpn60_TCP1
2573:Ubiquitin
2519:Clusterin
2191:IPR002423
1685:205522841
913:Chaperone
891:LOC401329
658:prefoldin
610:).
469:Structure
420:B:210-380
89:PDOC00610
77:IPR002423
2853:Ataxin 3
2187:InterPro
2152:Archived
2125:Archived
2108:Archived
2081:Archived
2026:16526409
1923:Virology
1837:20603018
1796:21618995
1744:18987317
1677:19491934
1642:32339190
1602:PLOS ONE
1583:12628000
1534:12001964
1526:27775711
1347:40768099
1253:10328521
1245:14686103
1210:52923821
1202:30291170
1154:29696145
1098:30911678
907:See also
821:Examples
807:radicals
673:phage EL
588:Group II
514:origin:
504:bacteria
172:RCSB PDB
72:InterPro
2776:(CDC34)
2061:1347461
2018:9476895
1977:9556522
1943:4878023
1907:8633011
1875:Bibcode
1845:3859016
1787:3132998
1735:2579888
1712:Bibcode
1633:7185714
1610:Bibcode
1574:1223359
1491:4341993
1483:7935790
1463:Bibcode
1440:1672279
1396:1350777
1339:1349837
1304:4325057
1296:2897629
1276:Bibcode
1145:5904260
1089:6420498
1013:4341993
1005:7935790
985:Bibcode
882:KCNMB3L
809:within
788:in vivo
776:E. coli
772:E. coli
746:E. coli
734:eukarya
723:archaea
715:E. coli
623:archaea
621:and in
619:cytosol
573:RuBisCO
528:E. coli
490:Group I
133:cd00309
84:PROSITE
65:PF00118
2820:Cullin
2177:(MeSH)
2096:(MeSH)
2059:
2024:
2016:
1975:
1941:
1905:
1895:
1843:
1835:
1794:
1784:
1742:
1732:
1683:
1675:
1640:
1630:
1581:
1571:
1532:
1524:
1489:
1481:
1455:Nature
1438:
1394:
1387:206108
1384:
1345:
1337:
1302:
1294:
1268:Nature
1251:
1243:
1208:
1200:
1152:
1142:
1128:: 31.
1096:
1086:
1011:
1003:
977:Nature
901:PIP5K3
887:CCT8L1
566:ATPase
187:PDBsum
161:
151:
121:SUPFAM
51:Symbol
3011:ATG12
3001:FAT10
2991:NEDD8
2976:ISG15
2969:Other
2958:PIAS4
2953:PIAS3
2948:PIAS2
2943:PIAS1
2893:(UBL)
2875:BIRC6
2835:FANCL
2507:Other
2496:TRAP1
2465:Hsp90
2391:Hsp70
2280:GroEL
2276:HSP60
2271:Hsp47
2266:Hsp27
2122:HSP60
2022:S2CID
1898:39481
1841:S2CID
1681:S2CID
1530:S2CID
1487:S2CID
1343:S2CID
1300:S2CID
1249:S2CID
1206:S2CID
1009:S2CID
929:Notes
877:HSPD1
872:CESK1
859:CCT6B
855:CCT6A
830:BBS10
784:GroEL
780:GroES
712:from
710:GroEL
546:GroES
536:GroEL
431:HSP60
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3016:FUB1
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2986:UFM1
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1973:PMID
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149:Pfam
113:1grl
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2825:CBL
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2808:E3
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2582:E1
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2382:C19
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2317:B11
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2004:doi
1931:doi
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1823:doi
1819:142
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1774:doi
1770:133
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1720:doi
1708:105
1665:doi
1628:PMC
1618:doi
1569:PMC
1561:doi
1557:371
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1471:doi
1459:371
1426:doi
1382:PMC
1374:doi
1370:174
1327:doi
1284:doi
1272:333
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1188:hdl
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