PDBsum entry 4d82

Hydrolase

PDB id: 4d82

Contents

Protein chains

267 a.a.

Ligands

ADP ×3

Waters ×12

PDB id:

4d82

Name:

Hydrolase

Title:

Metallosphera sedula vps4 crystal structure

Structure:

Aaa atpase, central domain protein. Chain: a, b, c. Fragment: aaa, unp residues 75-369. Engineered: yes. Other_details: truncation of the residues 1-74

Source:

Metallosphaera sedula. Organism_taxid: 43687. Gene: ha72_1672. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: c41.

Resolution:

3.20Å R-factor: 0.230 R-free: 0.268

Authors:

C.Caillat,P.Macheboeuf,Y.Wu,A.A.Mccarthy,E.Boeri-Erba,G.Effantin, H.G.Gottlinger,W.Weissenhorn,P.Renesto

Key ref:

C.Caillat et al. (2015). Asymmetric ring structure of Vps4 required for ESCRT-III disassembly. Nat Commun, 6, 8781. PubMed id: 26632262 DOI: 10.1038/ncomms9781

Date:

02-Dec-14 Release date: 25-Nov-15

Protein chains

A4YHC5  (A4YHC5_METS5) -  AAA ATPase, central domain protein from Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

Seq: 369 a.a.

Struc: 267 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/ncomms9781

Nat Commun 6:8781 (2015)

PubMed id: 26632262

Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.

C.Caillat, P.Macheboeuf, Y.Wu, A.A.McCarthy, E.Boeri-Erba, G.Effantin, H.G.Göttlinger, W.Weissenhorn, P.Renesto.

ABSTRACT

The vacuolar protein sorting 4 AAA-ATPase (Vps4) recycles endosomal sorting complexes required for transport (ESCRT-III) polymers from cellular membranes. Here we present a 3.6-Å X-ray structure of ring-shaped Vps4 from Metallosphera sedula (MsVps4), seen as an asymmetric pseudohexamer. Conserved key interface residues are shown to be important for MsVps4 assembly, ATPase activity in vitro, ESCRT-III disassembly in vitro and HIV-1 budding. ADP binding leads to conformational changes within the protomer, which might propagate within the ring structure. All ATP-binding sites are accessible and the pseudohexamer binds six ATP with micromolar affinity in vitro. In contrast, ADP occupies one high-affinity and five low-affinity binding sites in vitro, consistent with conformational asymmetry induced on ATP hydrolysis. The structure represents a snapshot of an assembled Vps4 conformation and provides insight into the molecular motions the ring structure undergoes in a concerted action to couple ATP hydrolysis to ESCRT-III substrate disassembly.