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. 2020 Jun 23;8:510. doi: 10.3389/fcell.2020.00510

FIGURE 2.

FIGURE 2

Structure of the yeast V-ATPase holoenzyme. (A) Cryo-electron micrograph structure of the assembled yeast V1-Vo complex (Zhao et al., 2015). A combination of the electron density and a chain trace of the different subunits is used to demonstrate the structural features of the V-ATPase holoenzyme. The subunits and distinct domains are indicated. The three distinct EG heterodimers (green and purple) are indicated by numbers on the side of the respective heterodimers. Upper-case letters indicate the subunit of the V1 sector and lower-cases represent the Vo-sector subunits. (B) A cartoon of the V-ATPase holoenzyme together with the functions performed by the V1 and the Vo sectors is demonstrated. Precisely, the V1 sector performs the ATP hydrolysis which is coupled to the proton transport function of the Vo sector. The direction of rotation of the rotor subunits (c8c′c″dDF) is indicated by a circular arrow on the hetero-decameric c-ring (cc′c″).

HHS Vulnerability Disclosure