3lca: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lca RCSB], [http://www.ebi.ac.uk/pdbsum/3lca PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lca RCSB], [http://www.ebi.ac.uk/pdbsum/3lca PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/TOM71_YEAST TOM71_YEAST]] Involved in MBF1-mediated mitochondrial morphogenesis.<ref>PMID:18007655</ref> [[http://www.uniprot.org/uniprot/HSP71_YEAST HSP71_YEAST]] May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.<ref>PMID:12761219</ref> | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 14:38, 25 December 2014
Structure of Tom71 complexed with Hsp70 Ssa1 C terminal tail indicating conformational plasticityStructure of Tom71 complexed with Hsp70 Ssa1 C terminal tail indicating conformational plasticity
Structural highlights
Function[TOM71_YEAST] Involved in MBF1-mediated mitochondrial morphogenesis.[1] [HSP71_YEAST] May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.[2] Publication Abstract from PubMedMitochondrial precursors are transported through the translocase of the outer membrane (TOM) complex. Tom70/Tom71 is a major surface receptor of the TOM complex for mitochondrial precursors and facilitates Hsp70/Hsp90-escorted precursor translocation into the mitochondrion. Previous structural studies of Tom71 have revealed that it contains an N-terminal and a C-terminal domain and that the two domains may remain in an open conformation when binding to Hsp70/Hsp90. In a newly obtained crystal form of a complex of Tom71 and the Hsp70 C-terminus, the N-terminal domain was found to have rotated about 12 degrees towards the C-terminal domain compared with the previous determined crystal structure of Tom71 in the open conformation. This newly solved structure is defined as the ;intermediate conformation'. The domain rearrangements in Tom71 significantly change the surface hydrophobicity and the volume of the precursor-binding pocket. This work suggests that Tom70/Tom71-family members may exhibit structural plasticity from the intermediate conformation to the fully open conformation when complexed with Hsp70/Hsp90. This structural plasticity enables the precursor receptors to accommodate different precursor substrates for mitochondrial translocation. The structural plasticity of Tom71 for mitochondrial precursor translocations.,Li J, Cui W, Sha B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):985-9. Epub 2010 Aug 21. PMID:20823510[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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