6bmf: Difference between revisions

Revision as of 02:24, 11 April 2020

Vps4p-Vta1p complex with peptide binding to the central pore of Vps4pVps4p-Vta1p complex with peptide binding to the central pore of Vps4p

6bmf, resolution 3.20Å

Structural highlights

6bmf is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Experimental data:	Check
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zahn R, Stevenson BJ, Schroder-Kohne S, Zanolari B, Riezman H, Munn AL. End13p/Vps4p is required for efficient transport from early to late endosomes in Saccharomyces cerevisiae. J Cell Sci. 2001 May;114(Pt 10):1935-47. PMID:11329380
↑ Babst M, Sato TK, Banta LM, Emr SD. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 1997 Apr 15;16(8):1820-31. PMID:9155008 doi:10.1093/emboj/16.8.1820
↑ Babst M, Wendland B, Estepa EJ, Emr SD. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 1998 Jun 1;17(11):2982-93. PMID:9606181 doi:10.1093/emboj/17.11.2982
↑ Han H, Monroe N, Sundquist WI, Shen PS, Hill CP. The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets. Elife. 2017 Nov 22;6. doi: 10.7554/eLife.31324. PMID:29165244 doi:http://dx.doi.org/10.7554/eLife.31324

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OCA

[1] Zahn R, Stevenson BJ, Schroder-Kohne S, Zanolari B, Riezman H, Munn AL. End13p/Vps4p is required for efficient transport from early to late endosomes in Saccharomyces cerevisiae. J Cell Sci. 2001 May;114(Pt 10):1935-47. PMID:11329380

[2] Babst M, Sato TK, Banta LM, Emr SD. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 1997 Apr 15;16(8):1820-31. PMID:9155008 doi:10.1093/emboj/16.8.1820

[3] Babst M, Wendland B, Estepa EJ, Emr SD. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 1998 Jun 1;17(11):2982-93. PMID:9606181 doi:10.1093/emboj/17.11.2982

[4] Han H, Monroe N, Sundquist WI, Shen PS, Hill CP. The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets. Elife. 2017 Nov 22;6. doi: 10.7554/eLife.31324. PMID:29165244 doi:http://dx.doi.org/10.7554/eLife.31324

[1]

[2]

[3]

[4]

@@ Line 3: / Line 3: @@
 <SX load='6bmf' size='340' side='right' viewer='molstar' caption='[[6bmf]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6bmf]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BMF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6bmf]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BMF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6BMF 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>
+</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='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=6bmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bmf OCA], [http://pdbe.org/6bmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bmf RCSB], [http://www.ebi.ac.uk/pdbsum/6bmf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bmf ProSAT]</span></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=6bmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bmf OCA], [http://pdbe.org/6bmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bmf RCSB], [http://www.ebi.ac.uk/pdbsum/6bmf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bmf ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[Vacuolar protein sorting-associated protein|Vacuolar protein sorting-associated protein]]
+*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
 == References ==
 <references/>

6bmf: Difference between revisions

Revision as of 02:24, 11 April 2020

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

Publication Abstract from PubMed

See Also

References

Contents

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6bmf: Difference between revisions

Revision as of 02:24, 11 April 2020

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

Publication Abstract from PubMed

See Also

References

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

Navigation menu

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