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-Structure paper
Title | Structure of the vacuolar H+-ATPase rotary motor reveals new mechanistic insights. |
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Journal, issue, pages | Structure, Vol. 23, Issue 3, Page 461-471, Year 2015 |
Publish date | Mar 3, 2015 |
Authors | Shaun Rawson / Clair Phillips / Markus Huss / Felix Tiburcy / Helmut Wieczorek / John Trinick / Michael A Harrison / Stephen P Muench / |
PubMed Abstract | Vacuolar H(+)-ATPases are multisubunit complexes that operate with rotary mechanics and are essential for membrane proton transport throughout eukaryotes. Here we report a ∼ 1 nm resolution ...Vacuolar H(+)-ATPases are multisubunit complexes that operate with rotary mechanics and are essential for membrane proton transport throughout eukaryotes. Here we report a ∼ 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. |
External links | Structure / PubMed:25661654 / PubMed Central |
Methods | EM (single particle) |
Resolution | 9.4 Å |
Structure data | EMDB-2781: |
Source |
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