RT Journal Article
SR Electronic
T1 The mechanical inhibition of the isolated V<sub>o</sub> from V-ATPase for proton conductance
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.02.13.946640
DO 10.1101/2020.02.13.946640
A1 Jun-ichi Kishikawa
A1 Atsuko Nakanishi
A1 Aya Furuta
A1 Takayuki Kato
A1 Keiichi Namba
A1 Masatada Tamakoshi
A1 Kaoru Mitsuoka
A1 Ken Yokoyama
YR 2020
UL http://biorxiv.org/content/early/2020/02/13/2020.02.13.946640.abstract
AB V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 moiety, with proton flow through the Vo membrane moiety, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo of eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the Vo is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the holo V/A-ATPase and the isolated Vo at near-atomic resolution, respectively. These structures clarify how the isolated Vo adopts the auto-inhibited form and how the holo complex prevents the formation of this inhibited Vo form.One Sentence Summary Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H+ translocation in the Vo membrane domain.