期刊
STRUCTURE
卷 23, 期 3, 页码 461-471出版社
CELL PRESS
DOI: 10.1016/j.str.2014.12.016
关键词
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资金
- MRC career development grant [G100567]
- Deutsche Forschungsgemeinschaft [SFB 944]
- Medical Research Council [G1000567] Funding Source: researchfish
- MRC [G1000567] Funding Source: UKRI
Vacuolar H+-ATPases are multisubunit complexes that operate with rotary mechanics and are essential for membrane proton transport throughout eukaryotes. Here we report a similar to 1 nm resolution reconstruction of a V-ATPase in a different conformational state from that previously reported for a lower-resolution yeast model. The stator network of the V-ATPase (and by implication that of other rotary ATPases) does not change conformation in different catalytic states, and hence must be relatively rigid. We also demonstrate that a conserved bearing in the catalytic domain is electrostatic, contributing to the extraordinarily high efficiency of rotary ATPases. Analysis of the rotor axle/membrane pump interface suggests how rotary ATPases accommodate different c ring stoichiometries while maintaining high efficiency. The model provides evidence for a half channel in the proton pump, supporting theoretical models of ion translocation. Our refined model therefore provides new insights into the structure and mechanics of the V-ATPases.
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