View source for 9bl8


==MIT (L7C/A43C) Domain of Vps4p==
<StructureSection load='9bl8' size='340' side='right'caption='[[9bl8]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BL8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=9bl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bl8 OCA], [https://pdbe.org/9bl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bl8 RCSB], [https://www.ebi.ac.uk/pdbsum/9bl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bl8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VPS4_YEAST VPS4_YEAST] Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.<ref>PMID:11329380</ref> <ref>PMID:9155008</ref> <ref>PMID:9606181</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ESCRT pathway's AAA+ ATPase, Vps4p, remodels ESCRT-III complexes to drive membrane fission. Here, we use peptide binding assays to further the understanding of substrate specificity and the mechanism of autoinhibition. Our results reveal unexpected sequence preference to the substrate binding groove and an elegant mechanism of regulation that couples localization to substrate with release from autoinhibition.

Vps4 substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition.,Wienkers HJ, Han H, Whitby FG, Hill CP bioRxiv [Preprint]. 2024 Sep 7:2024.09.07.611824. doi: 10.1101/2024.09.07.611824. PMID:39282404<ref>PMID:39282404</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9bl8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Han H]]
[[Category: Hill CP]]
[[Category: Whitby FG]]
[[Category: Wienkers HJ]]