 |
PDBsum entry 4d82
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Asymmetric ring structure of vps4 required for escrt-Iii disassembly.
|
|
|
Authors
|
|
C.Caillat,
P.Macheboeuf,
Y.Wu,
A.A.Mccarthy,
E.Boeri-Erba,
G.Effantin,
H.G.Göttlinger,
W.Weissenhorn,
P.Renesto.
|
|
|
Ref.
|
|
Nat Commun, 2015,
6,
8781.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
