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PDBsum entry 4d80
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PDB id:
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Hydrolase
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Title:
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Metallosphera sedula vps4 crystal structure
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Structure:
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Aaa atpase, central domain protein. Chain: a, b, c, d, e, f. Fragment: aaa, unp residues 75-369. Synonym: vps4. Engineered: yes. Other_details: truncation of the nterminus 74 residues
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Source:
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Metallosphaera sedula. Organism_taxid: 43687. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: c41.
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Resolution:
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3.60Å
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R-factor:
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0.267
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R-free:
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0.318
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Authors:
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C.Caillat,P.Macheboeuf,Y.Wu,A.A.Mccarthy,E.Boeri-Erba,G.Effantin, H.G.Gottlinger,W.Weissenhorn,P.Renesto
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Key ref:
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C.Caillat
et al.
(2015).
Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.
Nat Commun,
6,
8781.
PubMed id:
DOI:
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Date:
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02-Dec-14
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Release date:
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28-Oct-15
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PROCHECK
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Headers
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References
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A4YHC5
(A4YHC5_METS5) -
AAA ATPase, central domain protein from Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
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Seq:
Struc:
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369 a.a.
269 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.6.4.6
- vesicle-fusing ATPase.
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Reaction:
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ATP + H2O = ADP + phosphate + H+
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ATP
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+
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H2O
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=
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ADP
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+
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phosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Nat Commun
6:8781
(2015)
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PubMed id:
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Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.
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C.Caillat,
P.Macheboeuf,
Y.Wu,
A.A.McCarthy,
E.Boeri-Erba,
G.Effantin,
H.G.Göttlinger,
W.Weissenhorn,
P.Renesto.
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ABSTRACT
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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.
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