H+-translocating V-type ATPase. The 3-D structure is known (Lau and Rubinstein, 2012). More recently, Zhou and Sazanov 2019 solved cryo-EM structures of the intact Thermus thermophilus V/A-ATPase in three rotational
states with two substates. These structures indicate substantial
flexibility between V1 and Vo in a working enzyme,
which results from mechanical competition between central shaft
rotation and resistance from the peripheral stalks.
|Species:||Thermus thermophilus  |
|Number of TMSs:||3|
|Location1 / Topology2 / Orientation3:
Cell inner membrane1 / Peripheral membrane protein2
C:proton-transporting V-type ATPase, V0 domain
F:hydrogen ion transmembrane transporter acti...
P:ATP synthesis coupled proton transport
 “V-type H+-ATPase/synthase from a thermophilic eubacterium, Thermus thermophilus. Subunit structure and operon.” Yokoyama K.et.al. 10788522
1: MKKLLVTVLL AVFGALAFAA EEAAASGGLD RGLIAVGMGL AVGLAALGTG VAQARIGAAG
61: VGAIAEDRSN FGTALIFLLL PETLVIFGLL IAFILNGRL