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TIM/TOM complex

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The ATPase domain is essential during the interactions of the proteins Hsp70 and subunit Tim44. Without the presence of ATPase, carboxy-terminal segment is not able to bind to protein of Tim44. As mtHsp70 transmits the nucleotide state of the ATPase domain with alpha-helices A and B, Tim44 interacts
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Simplified representation of the Mitochondrial DNA Organization proteins (top image). A close up of a single ribosome in coordination with the TOM complex on the outer Mitochondrial membrane and the TIM complex on the inner Mitochondrial membrane (bottom image). The nascent transmembrane protein is
286:(TIM) complex, which are hypothesized to be transiently linked at sites of close contact between the two membranes. The signal sequence is then translocated into the matrix in a process that requires an electrochemical hydrogen ion gradient across the inner membrane. Mitochondrial 306:
located on the inner and outer membranes of the chloroplast, in the sense that it transports proteins into the membrane of the mitochondria. Although they both hydrolyze triphosphates, they are evolutionally unrelated.
341:"Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role" 176: 610: 1444: 501:"The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system" 195: 270:
and synthesised in the cytoplasm. These are tagged by an N-terminal or/and a C-terminal signal sequence. Following transport through the
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Voos W, Martin H, Krimmer T, Pfanner N (November 1999). "Mechanisms of protein translocation into mitochondria".
458:"Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane" 1388: 133: 115: 1658: 1410: 290:
binds to regions of the polypeptide chain and maintains it in an unfolded state as it moves into the matrix.
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Moro, Fernando; Okamoto, Koji; Donzeau, Mariel; Neupert, Walter; Brunner, Michael (2002-03-01).
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Berthold J, Bauer MF, Schneider HC, Klaus C, Dietmeier K, Neupert W, Brunner M (June 1995).
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being fed into the mitochondrial membrane where its target peptide (not shown) gets cleaved.
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Bömer U, Meijer M, Maarse AC, Hönlinger A, Dekker PJ, Pfanner N, Rassow J (May 1997).
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from the nucleus, the signal sequence is recognized by a receptor protein in the
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Krimmer, T.; Rassow, J.; Kunau, W. H.; Voos, W.; Pfanner, N. (2000-08-01).
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chain are inserted in the TOM complex, then begin interaction with a
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B. Alberts, A. Johnson, J. Lewis, M. Raff,. K. Roberts, P. Walter.
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with the peptide binding domain to coordinate the protein bind.
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Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes
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This protein complex is functionally analogous to the
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ATP phosphohydrolase (mitochondrial protein-importing)
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Overview of the various import ways into mitochondria
1855: 228:through the mitochondrial membrane for use in 1838: 1496: 604: 1845: 1831: 1503: 1489: 611: 597: 516: 481: 413: 372: 238:mitochondrial protein-transporting ATPase 28:mitochondrial protein-transporting ATPase 15: 446:Toc, Tic and chloroplast protein import 1856: 1484: 592: 1797: 334: 332: 575:- description of the entire complex 402:The Journal of Biological Chemistry 298:TIC/TOC Complex vs. TIM/TOM Complex 13: 14: 1905: 563: 329: 284:translocase of the inner membrane 276:translocase of the outer membrane 258:Only 13 proteins necessary for a 236:, the complex is described as an 216:is a protein complex in cellular 1801: 1781: 357:10.1128/mcb.20.16.5879-5887.2000 438: 389: 345:Molecular and Cellular Biology 317: 1: 548:10.1016/s0304-4157(99)00007-6 518:10.1016/S0092-8674(05)80013-3 325:Molecular Biology of the Cell 310: 1889:Enzymes of unknown structure 1817:. You can help Knowledge by 7: 1510: 1381:Protein-synthesizing GTPase 251:, as the TIM part requires 10: 1910: 1796: 247:), or more systematically 1667: 1659:Michaelis–Menten kinetics 1631: 1600: 1569: 1518: 1440:Guanylate-binding protein 1419: 1378: 1118: 992: 979: 944: 896: 877: 823: 743: 722: 715: 698: 675: 635: 624:acid anhydride hydrolases 230:oxidative phosphorylation 194: 182: 170: 165: 161: 145: 126: 114: 102: 90: 78: 66: 54: 49: 37: 32: 27: 1551:Diffusion-limited enzyme 995:Heterotrimeric G protein 690:Phosphoadenylylsulfatase 667:Thiamine-triphosphatase 474:10.1093/emboj/16.9.2205 1874:Transmembrane proteins 1813:-related article is a 415:10.1074/jbc.M107935200 262:are actually coded in 224:produced from nuclear 22: 1644:Eadie–Hofstee diagram 1577:Allosteric regulation 1422:Polymerization motors 1133:Rho family of GTPases 581:(group of N. Pfanner) 19: 1654:Lineweaver–Burk plot 444:P. Jarvis, J. Soll, 255:hydrolysis to work. 1430:dynamin superfamily 220:which translocates 1864:Transport proteins 1613:Enzyme superfamily 1546:Enzyme promiscuity 23: 1826: 1825: 1769: 1768: 1478: 1477: 1474: 1473: 975: 974: 940: 939: 685:Adenylylsulfatase 351:(16): 5879–5887. 264:mitochondrial DNA 210: 209: 206: 205: 109:metabolic pathway 1901: 1847: 1840: 1833: 1805: 1798: 1786: 1785: 1777: 1649:Hanes–Woolf plot 1592:Enzyme activator 1587:Enzyme inhibitor 1561:Enzyme catalysis 1505: 1498: 1491: 1482: 1481: 990: 989: 720: 719: 713: 712: 613: 606: 599: 590: 589: 559: 530: 520: 495: 485: 462:The EMBO Journal 448: 442: 436: 435: 417: 408:(9): 6874–6880. 393: 387: 386: 376: 336: 327: 321: 163: 162: 25: 24: 1909: 1908: 1904: 1903: 1902: 1900: 1899: 1898: 1854: 1853: 1852: 1851: 1794: 1792: 1780: 1772: 1770: 1765: 1677:Oxidoreductases 1663: 1639:Enzyme kinetics 1627: 1623:List of enzymes 1596: 1565: 1536:Catalytic triad 1514: 1509: 1479: 1470: 1415: 1374: 1125:Ras superfamily 1114: 1098: 1078: 1024: 1014: 1006: 971: 936: 892: 873: 819: 776:Plasma membrane 739: 694: 671: 645:Pyrophosphatase 631: 617: 566: 452: 451: 443: 439: 394: 390: 337: 330: 322: 318: 313: 304:TIC/TOC complex 300: 214:TIM/TOM complex 12: 11: 5: 1907: 1897: 1896: 1891: 1886: 1881: 1876: 1871: 1866: 1850: 1849: 1842: 1835: 1827: 1824: 1823: 1806: 1791: 1790: 1767: 1766: 1764: 1763: 1750: 1737: 1724: 1711: 1698: 1685: 1671: 1669: 1665: 1664: 1662: 1661: 1656: 1651: 1646: 1641: 1635: 1633: 1629: 1628: 1626: 1625: 1620: 1615: 1610: 1604: 1602: 1601:Classification 1598: 1597: 1595: 1594: 1589: 1584: 1579: 1573: 1571: 1567: 1566: 1564: 1563: 1558: 1553: 1548: 1543: 1538: 1533: 1528: 1522: 1520: 1516: 1515: 1508: 1507: 1500: 1493: 1485: 1476: 1475: 1472: 1471: 1469: 1468: 1463: 1462: 1461: 1456: 1447: 1442: 1437: 1426: 1424: 1417: 1416: 1414: 1413: 1408: 1407: 1406: 1401: 1396: 1385: 1383: 1376: 1375: 1373: 1372: 1367: 1362: 1357: 1352: 1351: 1350: 1345: 1340: 1335: 1325: 1324: 1323: 1318: 1308: 1307: 1306: 1301: 1296: 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401: 391: 348: 344: 324: 319: 301: 292: 257: 248: 237: 218:biochemistry 213: 211: 73:BRENDA entry 1526:Active site 1445:Mitofusin-1 1420:3.6.5.5-6: 1389:Prokaryotic 280:polypeptide 61:IntEnz view 33:Identifiers 1858:Categories 1729:Isomerases 1703:Hydrolases 1570:Regulation 1411:Eukaryotic 1044:Transducin 881:(3.6.3.10) 620:Hydrolases 311:References 234:enzymology 130:structures 97:KEGG entry 1608:EC number 1379:3.6.5.3: 1119:3.6.5.2: 1061:Gustducin 993:3.6.5.1: 827:(3.6.3.9) 747:(3.6.3.8) 650:Inorganic 424:0021-9258 365:0270-7306 50:Databases 1884:EC 7.4.2 1879:EC 3.6.3 1632:Kinetics 1556:Cofactor 1519:Activity 655:Thiamine 556:10548718 432:11733493 383:10913171 222:proteins 201:proteins 189:articles 177:articles 134:RCSB PDB 1788:Biology 1742:Ligases 1512:Enzymes 1466:Tubulin 1435:Dynamin 1287:other: 967:Katanin 957:Kinesin 932:ATP13A3 927:ATP13A2 662:Apyrase 527:7600576 492:9171336 483:1169823 272:cytosol 268:nucleus 245:7.4.2.3 156:QuickGO 121:profile 104:MetaCyc 44:7.4.2.3 1811:enzyme 1774:Portal 1716:Lyases 1343:ARL13B 1203:RhoBTB 1097:α12/13 985:GTPase 962:Myosin 952:Dynein 922:ATP12A 917:ATP11B 912:ATP10A 907:ATP8B1 897:Other 869:ATP1B4 864:ATP1B3 859:ATP1B2 854:ATP1B1 849:ATP1A4 844:ATP1A3 839:ATP1A2 834:ATP1A1 825:Na+/K+ 813:ATP2C2 808:ATP2C1 796:ATP2B4 791:ATP2B3 786:ATP2B2 781:ATP2B1 769:ATP2A3 764:ATP2A2 759:ATP2A1 708:ATPase 554:  525:  490:  480:  430:  422:  381:  371:  363:  184:PubMed 166:Search 152:AmiGO 140:PDBsum 80:ExPASy 68:BRENDA 56:IntEnz 39:EC no. 1809:This 1668:Types 1399:EF-Tu 1338:SAR1B 1321:RAB27 1316:RAB23 1269:RhoDF 1159:RhoUV 1142:CDC42 1137:Cdc42 1123:> 1108:GNA13 1103:GNA12 1088:GNA11 1077:αq/11 1066:GNAT3 1054:GNAT2 1049:GNAT1 1039:GNAI3 1034:GNAI2 1029:GNAI1 981:3.6.5 945:3.6.4 888:ATP4A 879:H+/K+ 754:SERCA 716:3.6.3 700:3.6.3 677:3.6.2 637:3.6.1 573:3.A.8 374:86065 288:Hsp70 232:. In 116:PRIAM 1815:stub 1760:list 1753:EC7 1747:list 1740:EC6 1734:list 1727:EC5 1721:list 1714:EC4 1708:list 1701:EC3 1695:list 1688:EC2 1682:list 1675:EC1 1459:OPA1 1452:and 1404:EF-G 1394:IF-2 1360:Rheb 1348:ARL6 1333:ARF6 1304:NRAS 1299:KRAS 1294:HRAS 1279:RhoD 1274:RhoF 1220:RhoH 1196:RhoG 1181:Rac1 1169:RhoV 1164:RhoU 1147:TC10 1083:GNAQ 803:SPCA 630:3.6) 570:TCDB 552:PMID 540:1422 523:PMID 505:Cell 488:PMID 428:PMID 420:ISSN 379:PMID 361:ISSN 212:The 196:NCBI 137:PDBe 92:KEGG 1454:MX2 1450:MX1 1370:RGK 1365:Rap 1355:Ran 1328:Arf 1311:Rab 1289:Ras 1247:Rnd 1225:Rho 1176:Rac 1152:TCL 1013:olf 745:Ca+ 544:doi 513:doi 478:PMC 470:doi 410:doi 406:277 369:PMC 353:doi 253:ATP 226:DNA 172:PMC 128:PDB 1860:: 1135:: 1023:αi 1005:αs 983:: 706:: 628:EC 622:: 550:. 538:. 521:. 509:81 507:. 503:. 486:. 476:. 466:16 464:. 460:. 426:. 418:. 404:. 400:. 377:. 367:. 359:. 349:20 347:. 343:. 331:^ 242:EC 154:/ 1846:e 1839:t 1832:v 1821:. 1776:: 1762:) 1758:( 1749:) 1745:( 1736:) 1732:( 1723:) 1719:( 1710:) 1706:( 1697:) 1693:( 1684:) 1680:( 1504:e 1497:t 1490:v 1262:3 1257:2 1252:1 1240:C 1235:B 1230:A 1213:2 1208:1 1191:3 1186:2 1095:G 1075:G 1021:G 1011:G 1003:G 704:4 702:- 626:( 612:e 605:t 598:v 558:. 546:: 529:. 515:: 494:. 472:: 434:. 412:: 385:. 355:: 240:(

Index


EC no.
7.4.2.3
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
Gene Ontology
AmiGO
QuickGO
PMC
articles
PubMed
articles
NCBI
proteins
biochemistry
proteins

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