4D80

Metallosphera sedula Vps4 crystal structure

4D80 の概要

• エントリーDOI: 10.2210/pdb4d80/pdb
• 分子名称: AAA ATPASE, CENTRAL DOMAIN PROTEIN (1 entity in total)
• 機能のキーワード: hydrolase, atpase
• 由来する生物種: METALLOSPHAERA SEDULA
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 216693.07

構造登録者

Caillat, C.,Macheboeuf, P.,Wu, Y.,McCarthy, A.A.,Boeri-Erba, E.,Effantin, G.,Gottlinger, H.G.,Weissenhorn, W.,Renesto, P. (登録日: 2014-12-02, 公開日: 2015-10-28, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.6 Å)