Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases

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Science Advances  22 Jul 2016:
Vol. 2, no. 7, e1600725
DOI: 10.1126/sciadv.1600725


  • Fig. 1 Subunit arrangement in three types of rotary ATPases.

    Schematic representations of T. thermophilus V/A-ATPase (A), S. cerevisiae V-ATPases (B), and B. taurus F-type ATP synthase (C) [adapted with permission from Schep et al. (71)]. OSCP, oligomycin sensitivity conferral protein.

  • Fig. 2 Rotational states of V-ATPase.

    (A to C) Three cryo-EM maps from the S. cerevisiae V-ATPase representing three distinct conformational states of the enzyme. Two upper and lower panels show cross sections through the different conformations. Scale bar, 25 Å [adapted with permission from Zhao et al. (24)].

  • Fig. 3 Model of proton translocation via the a-subunit.

    (A to C) A similar arrangement of residues is present in V/A-ATPase (A), V-ATPase (B), and F-type ATP synthase (C). Clusters of residues important for proton translocation are highlighted for the cytoplasmic half-channel (orange ellipse) and lumenal half-channel (blue ellipse). The conserved essential arginine residues are circled in black. (D) Schematic diagram of the half-channel model for proton translocation in the S. cerevisiae V-ATPase [adapted with permission from Schep et al. (71)].

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