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TitleMechanical inhibition of isolated V from V/A-ATPase for proton conductance.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJul 8, 2020
AuthorsJun-Ichi Kishikawa / Atsuko Nakanishi / Aya Furuta / Takayuki Kato / Keiichi Namba / Masatada Tamakoshi / Kaoru Mitsuoka / Ken Yokoyama /
PubMed AbstractV-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V domain, with proton flow through the V membrane domain, via rotation of the central rotor complex ...V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V domain, with proton flow through the V membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V domain, the V domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the V domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the V/A-ATPase and isolated V at near-atomic resolution, respectively. These structures clarify how the isolated V domain adopts the auto-inhibited form and how the complex prevents formation of the inhibited V form.
External linksElife / PubMed:32639230 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 3.93 Å
Structure data

EMDB-30013:
V/A-ATPase from Thermus thermophilus
Method: EM (single particle) / Resolution: 3.6 Å

30014

6ly8

EMDB-30014: V1-ATPase built from cryo-EM map of V/A-ATPase from Thermus thermophilus.
PDB-6ly8: V/A-ATPase from Thermus thermophilus, the soluble domain, including V1, d, two EG stalks, and N-terminal domain of a-subunit.
Method: EM (single particle) / Resolution: 3.5 Å

30015

6ly9

EMDB-30015, PDB-6ly9:
The membrane-embedded Vo domain of V/A-ATPase from Thermus thermophilus
Method: EM (single particle) / Resolution: 3.93 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • thermus thermophilus hb8 (bacteria)
KeywordsMOTOR PROTEIN / rotary ATPase / V/A-ATPase / molecular motor

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