4D82

Metallosphera sedula Vps4 crystal structure

Summary for 4D82

• Entry DOI: 10.2210/pdb4d82/pdb
• Related: 4D81
• Descriptor: AAA ATPase, central domain protein, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Metallosphaera sedula
• Total number of polymer chains: 3
• Total formula weight: 102137.75

Authors

Caillat, C.,Macheboeuf, P.,Wu, Y.,McCarthy, A.A.,Boeri-Erba, E.,Effantin, G.,Gottlinger, H.G.,Weissenhorn, W.,Renesto, P. (deposition date: 2014-12-02, release date: 2015-11-25, Last modification date: 2023-12-20)

Primary citation

Caillat, C.,Macheboeuf, P.,Wu, Y.,Mccarthy, A.A.,Boeri-Erba, E.,Effantin, G.,Gottlinger, H.G.,Weissenhorn, W.,Renesto, P.
Asymmetric Ring Structure of Vps4 Required for Escrt-III Disassembly.
Nat.Commun., 6:8781-, 2015

PubMed 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.

PubMed: 26632262
DOI: 10.1038/NCOMMS9781

Experimental method

X-RAY DIFFRACTION (3.2 Å)