6ap1: Difference between revisions
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==Vps4p-Vta1p complex with peptide binding to the central pore of Vps4p== | |||
<StructureSection load='6ap1' size='340' side='right' caption='[[6ap1]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ap1]] is a 19 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AP1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AP1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=6ap1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ap1 OCA], [http://pdbe.org/6ap1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ap1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ap1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ap1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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> [[http://www.uniprot.org/uniprot/VTA1_YEAST VTA1_YEAST]] Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase activity by 6- to 8-fold.<ref>PMID:12953057</ref> <ref>PMID:14701806</ref> <ref>PMID:16505166</ref> <ref>PMID:16601096</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The hexameric AAA ATPase Vps4 drives membrane fission by remodeling and disassembling ESCRT-III filaments. Building upon our earlier 4.3 A resolution cryo-EM structure (Monroe et al., 2017), we now report a 3.2 A structure of Vps4 bound to an ESCRT-III peptide substrate. The new structure reveals that the peptide approximates a beta-strand conformation whose helical symmetry matches that of the five Vps4 subunits it contacts directly. Adjacent Vps4 subunits make equivalent interactions with successive substrate dipeptides through two distinct classes of side chain binding pockets formed primarily by Vps4 pore loop 1. These pockets accommodate a wide range of residues, while main chain hydrogen bonds may help dictate substrate-binding orientation. The structure supports a 'conveyor belt' model of translocation in which ATP binding allows a Vps4 subunit to join the growing end of the helix and engage the substrate, while hydrolysis and release promotes helix disassembly and substrate release at the lagging end. | |||
The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets.,Han H, Monroe N, Sundquist WI, Shen PS, Hill CP Elife. 2017 Nov 22;6. doi: 10.7554/eLife.31324. PMID:29165244<ref>PMID:29165244</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ap1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Han, H]] | |||
[[Category: Hill, C P]] | |||
[[Category: Monroe, N]] | |||
[[Category: Shen, P]] | |||
[[Category: Sundquist, W I]] | |||
[[Category: Aaa atpase]] | |||
[[Category: Escrt]] | |||
[[Category: Transport protein]] | |||
[[Category: Vps4]] | |||
[[Category: Vta1]] | |||
Revision as of 10:23, 6 December 2017
Vps4p-Vta1p complex with peptide binding to the central pore of Vps4pVps4p-Vta1p complex with peptide binding to the central pore of Vps4p
Structural highlights
Function[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.[1] [2] [3] [VTA1_YEAST] Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase activity by 6- to 8-fold.[4] [5] [6] [7] Publication Abstract from PubMedThe hexameric AAA ATPase Vps4 drives membrane fission by remodeling and disassembling ESCRT-III filaments. Building upon our earlier 4.3 A resolution cryo-EM structure (Monroe et al., 2017), we now report a 3.2 A structure of Vps4 bound to an ESCRT-III peptide substrate. The new structure reveals that the peptide approximates a beta-strand conformation whose helical symmetry matches that of the five Vps4 subunits it contacts directly. Adjacent Vps4 subunits make equivalent interactions with successive substrate dipeptides through two distinct classes of side chain binding pockets formed primarily by Vps4 pore loop 1. These pockets accommodate a wide range of residues, while main chain hydrogen bonds may help dictate substrate-binding orientation. The structure supports a 'conveyor belt' model of translocation in which ATP binding allows a Vps4 subunit to join the growing end of the helix and engage the substrate, while hydrolysis and release promotes helix disassembly and substrate release at the lagging end. The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets.,Han H, Monroe N, Sundquist WI, Shen PS, Hill CP Elife. 2017 Nov 22;6. doi: 10.7554/eLife.31324. PMID:29165244[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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