期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 41, 期 1, 页码 106-116出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2015.10.006
关键词
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资金
- Max Planck Society
- DFG Cluster of Excellence Macromolecular Complexes
Rotary ATPases are energy-converting nanomachines found in the membranes of all living organisms. The mechanism by which proton translocation through the membrane drives ATP synthesis, or how ATP hydrolysis generates a transmembrane proton gradient, has been unresolved for decades because the structure of a critical subunit in the membrane was unknown. Electron cryomicroscopy (cryoEM) studies of two rotary ATPases have now revealed a hairpin of long, horizontal, membrane-intrinsic a-helices in the a-subunit next to the c-ring rotor. The horizontal helices create a pair of aqueous half-channels in the membrane that provide access to the proton-binding sites in the rotor ring. These recent findings help to explain the highly conserved mechanism of ion translocation by rotary ATPases.
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