| Autor: |
Rawson, S, Phillips, C, Huss, M, Tiburcy, F, Wieczorek, H, Trinick, J, Harrison, MA, Muench, SP |
| Jazyk: |
angličtina |
| Rok vydání: |
2015 |
| Předmět: |
|
| ISSN: |
0969-2126 |
| Popis: |
SummaryVacuolar 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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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