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6pdw

From Proteopedia

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Current revision (09:26, 20 March 2024) (edit) (undo)
 
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<SX load='6pdw' size='340' side='right' viewer='molstar' caption='[[6pdw]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<SX load='6pdw' size='340' side='right' viewer='molstar' caption='[[6pdw]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6pdw]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PDW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PDW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6pdw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PDW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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">Electron Microscopy, [[Resolution|Resolution]] 3.1&#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=UNK:UNKNOWN'>UNK</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6pdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pdw OCA], [http://pdbe.org/6pdw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pdw RCSB], [http://www.ebi.ac.uk/pdbsum/6pdw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pdw 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=6pdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pdw OCA], [https://pdbe.org/6pdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pdw RCSB], [https://www.ebi.ac.uk/pdbsum/6pdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pdw ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G0S654_CHATD G0S654_CHATD]
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The AAA protein Msp1 extracts mislocalized tail-anchored membrane proteins and targets them for degradation, thus maintaining proper cell organization. How Msp1 selects its substrates and firmly engages them during the energetically unfavorable extraction process remains a mystery. To address this question, we solved cryo-EM structures of Msp1-substrate complexes at near-atomic resolution. Akin to other AAA proteins, Msp1 forms hexameric spirals that translocate substrates through a central pore. A singular hydrophobic substrate recruitment site is exposed at the spiral's seam, which we propose positions the substrate for entry into the pore. There, a tight web of aromatic amino acids grips the substrate in a sequence-promiscuous, hydrophobic milieu. Elements at the intersubunit interfaces coordinate ATP hydrolysis with the subunits' positions in the spiral. We present a comprehensive model of Msp1's mechanism, which follows general architectural principles established for other AAA proteins yet specializes Msp1 for its unique role in membrane protein extraction.
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Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction.,Wang L, Myasnikov A, Pan X, Walter P Elife. 2020 Jan 30;9. pii: 54031. doi: 10.7554/eLife.54031. PMID:31999255<ref>PMID:31999255</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 6pdw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Chaetomium thermophilum]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myasnikov, A]]
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[[Category: Myasnikov A]]
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[[Category: Pan, X]]
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[[Category: Pan X]]
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[[Category: Walter, P]]
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[[Category: Walter P]]
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[[Category: Wang, L]]
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[[Category: Wang L]]
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[[Category: Membrane protein]]
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[[Category: Protein quality control]]
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[[Category: Protein transport]]
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[[Category: Tail-anchored protein]]
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Current revision

Msp1-substrate complex in closed conformation

6pdw, resolution 3.10Å

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