6pe0: Difference between revisions

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-'''Unreleased structure'''
-The entry 6pe0 is ON HOLD  until Paper Publication
+==Msp1 (E214Q)-substrate complex==
+<StructureSection load='6pe0' size='340' side='right'caption='[[6pe0]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6pe0]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PE0 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<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>
+<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=6pe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pe0 OCA], [http://pdbe.org/6pe0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pe0 RCSB], [http://www.ebi.ac.uk/pdbsum/6pe0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pe0 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6pe0" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Myasnikov, A]]
+[[Category: Pan, X]]
+[[Category: Walter, P]]
+[[Category: Wang, L]]
+[[Category: Membrane protein]]
+[[Category: Protein quality control]]
+[[Category: Protein transport]]
+[[Category: Tail-anchored protein]]