5whg

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==Vms1 mitochondrial localization core==
==Vms1 mitochondrial localization core==
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<StructureSection load='5whg' size='340' side='right' caption='[[5whg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='5whg' size='340' side='right'caption='[[5whg]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5whg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WHG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5whg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WHG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=5whg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5whg OCA], [http://pdbe.org/5whg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5whg RCSB], [http://www.ebi.ac.uk/pdbsum/5whg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5whg ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5whg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5whg OCA], [https://pdbe.org/5whg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5whg RCSB], [https://www.ebi.ac.uk/pdbsum/5whg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5whg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VMS1_YEAST VMS1_YEAST]] Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. Component of an evolutionarily conserved system for ubiquitin-mediated mitochondria-associated protein degradation (MAD), which is necessary to maintain mitochondrial, cellular, and organismal viability.<ref>PMID:21070972</ref> <ref>PMID:21148305</ref>
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[https://www.uniprot.org/uniprot/VMS1_YEAST VMS1_YEAST] Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. Component of an evolutionarily conserved system for ubiquitin-mediated mitochondria-associated protein degradation (MAD), which is necessary to maintain mitochondrial, cellular, and organismal viability.<ref>PMID:21070972</ref> <ref>PMID:21148305</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vms1 translocates to damaged mitochondria in response to stress, whereupon its binding partner, Cdc48, contributes to mitochondrial protein homeostasis. Mitochondrial targeting of Vms1 is mediated by its conserved mitochondrial targeting domain (MTD), which, in unstressed conditions, is inhibited by intramolecular binding to the Vms1 leucine-rich sequence (LRS). Here, we report a 2.7 A crystal structure of Vms1 that reveals that the LRS lies in a hydrophobic groove in the autoinhibited MTD. We also demonstrate that the oxidized sterol, ergosterol peroxide, is necessary and sufficient for Vms1 localization to mitochondria, through binding the MTD in an interaction that is competitive with binding to the LRS. These data support a model in which stressed mitochondria generate an oxidized sterol receptor that recruits Vms1 to support mitochondrial protein homeostasis.
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Sterol Oxidation Mediates Stress-Responsive Vms1 Translocation to Mitochondria.,Nielson JR, Fredrickson EK, Waller TC, Rendon OZ, Schubert HL, Lin Z, Hill CP, Rutter J Mol Cell. 2017 Nov 16;68(4):673-685.e6. doi: 10.1016/j.molcel.2017.10.022. PMID:29149595<ref>PMID:29149595</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5whg" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fredrickson, E K]]
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[[Category: Large Structures]]
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[[Category: Hill, C P]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Rutter, J]]
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[[Category: Fredrickson EK]]
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[[Category: Schubert, H L]]
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[[Category: Hill CP]]
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[[Category: Dna binding protein]]
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[[Category: Rutter J]]
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[[Category: Mitochondrial quality control]]
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[[Category: Schubert HL]]
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[[Category: Oxidative stress]]
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[[Category: Ros signalling]]
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Current revision

Vms1 mitochondrial localization core

PDB ID 5whg

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