3lca: Difference between revisions
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<StructureSection load='3lca' size='340' side='right'caption='[[3lca]], [[Resolution|resolution]] 2.19Å' scene=''> | <StructureSection load='3lca' size='340' side='right'caption='[[3lca]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3lca]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3lca]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LCA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lca OCA], [https://pdbe.org/3lca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lca RCSB], [https://www.ebi.ac.uk/pdbsum/3lca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lca ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TOM71_YEAST TOM71_YEAST]] Involved in MBF1-mediated mitochondrial morphogenesis.<ref>PMID:18007655</ref> [[https://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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 16:39, 4 May 2022
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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