6pdw: Difference between revisions

No edit summary
No edit summary
 
Line 3: Line 3:
<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 ==
<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>
<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>
</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>
</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>
<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='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>
<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>
<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>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/G0S654_CHATD G0S654_CHATD]
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 6pdw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Chaetomium thermophilum]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Myasnikov, A]]
[[Category: Myasnikov A]]
[[Category: Pan, X]]
[[Category: Pan X]]
[[Category: Walter, P]]
[[Category: Walter P]]
[[Category: Wang, L]]
[[Category: Wang L]]
[[Category: Membrane protein]]
[[Category: Protein quality control]]
[[Category: Protein transport]]
[[Category: Tail-anchored protein]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA