Structure of the Vacuolar H+-ATPase Rotary Motor Reveals New Mechanistic Insights

Autor(en): Rawson, Shaun 
Phillips, Clair 
Huss, Markus 
Tiburcy, Felix 
Wieczorek, Helmut 
Trinick, John 
Harrison, Michael A. 
Muench, Stephen P. 
Stichwörter: Biochemistry & Molecular Biology; Biophysics; Cell Biology; CENTRAL STALK; CRYSTAL-STRUCTURE; MEMBRANE TOPOLOGY; NA+-ATPASE; ROTOR RING; SUBUNIT-C; SYNTHASE; TRANSMEMBRANE SEGMENTS; V-ATPASE; YEAST
Erscheinungsdatum: 2015
Herausgeber: CELL PRESS
Journal: STRUCTURE
Volumen: 23
Ausgabe: 3
Startseite: 461
Seitenende: 471
Zusammenfassung: 
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.
ISSN: 09692126
DOI: 10.1016/j.str.2014.12.016

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