6BMF

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

Summary for 6BMF

• Entry DOI: 10.2210/pdb6bmf/pdb
• EMDB information: 8887
• Descriptor: Vacuolar protein sorting-associated protein 4, Vps2p, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: vps4, escrt, vta1, aaa atpase, transport protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Endosome membrane ; Peripheral membrane protein : P52917
• Total number of polymer chains: 6
• Total formula weight: 188989.12

Authors

Han, H.,Monroe, N.,Shen, P.,Sundquist, W.I.,Hill, C.P. (deposition date: 2017-11-14, release date: 2017-12-06, Last modification date: 2025-05-28)

Primary citation

Han, H.,Monroe, N.,Sundquist, W.I.,Shen, P.S.,Hill, C.P.
The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets.
Elife, 6:-, 2017

PubMed Abstract: The hexameric AAA ATPase Vps4 drives membrane fission by remodeling and disassembling ESCRT-III filaments. Building upon our earlier 4.3 Å resolution cryo-EM structure (Monroe et al., 2017), we now report a 3.2 Å structure of Vps4 bound to an ESCRT-III peptide substrate. The new structure reveals that the peptide approximates a β-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.

PubMed: 29165244
DOI: 10.7554/eLife.31324

Experimental method

ELECTRON MICROSCOPY (3.2 Å)