2guz
From Proteopedia
(Difference between revisions)
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<StructureSection load='2guz' size='340' side='right'caption='[[2guz]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2guz' size='340' side='right'caption='[[2guz]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2guz]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2guz]] is a 16 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=2GUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GUZ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | |
| - | <tr id=' | + | |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2guz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2guz OCA], [https://pdbe.org/2guz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2guz RCSB], [https://www.ebi.ac.uk/pdbsum/2guz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2guz ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2guz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2guz OCA], [https://pdbe.org/2guz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2guz RCSB], [https://www.ebi.ac.uk/pdbsum/2guz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2guz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/TIM14_YEAST TIM14_YEAST] Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1).<ref>PMID:14517234</ref> <ref>PMID:14638855</ref> <ref>PMID:14605210</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2guz ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2guz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The import motor of the mitochondrial translocase of the inner membrane (TIM23) mediates the ATP-dependent translocation of preproteins into the mitochondrial matrix by cycles of binding to and release from mtHsp70. An essential step of this process is the stimulation of the ATPase activity of mtHsp70 performed by the J cochaperone Tim14. Tim14 forms a complex with the J-like protein Tim16. The crystal structure of this complex shows that the conserved domains of the two proteins have virtually identical folds but completely different surfaces enabling them to perform different functions. The Tim14-Tim16 dimer reveals a previously undescribed arrangement of J and J-like domains. Mutations that destroy the complex between Tim14 and Tim16 are lethal demonstrating that complex formation is an essential requirement for the viability of cells. We further demonstrate tight regulation of the cochaperone activity of Tim14 by Tim16. The first crystal structure of a J domain in complex with a regulatory protein provides new insights into the function of the mitochondrial TIM23 translocase and the Hsp70 chaperone system in general. | ||
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| - | Structure and function of Tim14 and Tim16, the J and J-like components of the mitochondrial protein import motor.,Mokranjac D, Bourenkov G, Hell K, Neupert W, Groll M EMBO J. 2006 Oct 4;25(19):4675-85. Epub 2006 Sep 14. PMID:16977310<ref>PMID:16977310</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2guz" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bourenkov | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Groll | + | [[Category: Bourenkov G]] |
| - | [[Category: Hell | + | [[Category: Groll M]] |
| - | [[Category: Mokranjac | + | [[Category: Hell K]] |
| - | [[Category: Neupert | + | [[Category: Mokranjac D]] |
| - | + | [[Category: Neupert W]] | |
| - | + | ||
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Current revision
Structure of the Tim14-Tim16 complex of the mitochondrial protein import motor
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