View source for 6pe0


==Msp1 (E214Q)-substrate complex==
<SX load='6pe0' size='340' side='right' viewer='molstar' 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://proteopedia.org/fgij/fg.htm?mol=6PE0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://proteopedia.org/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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pe0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[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]]