3lca: Difference between revisions
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==Structure of Tom71 complexed with Hsp70 Ssa1 C terminal tail indicating conformational plasticity== | ==Structure of Tom71 complexed with Hsp70 Ssa1 C terminal tail indicating conformational plasticity== | ||
<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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LCA FirstGlance]. <br> | <table><tr><td colspan='2'>[[3lca]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LCA FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3lca" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3lca" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Li, J Z]] | [[Category: Li, J Z]] | ||
Revision as of 17:18, 25 December 2019
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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