Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 32, Issue 2, Pages 53-56Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2006.12.006
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Funding
- NIGMS NIH HHS [GM 076214, R01 GM071462-05] Funding Source: Medline
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ATP synthase synthesizes ATP from ADP and inorganic phosphate using a unique rotary mechanism whereby two subcomplexes move relative to each other, powered by a proton or sodium gradient. The non-rotating parts of the machinery are held together by the 'stator stalk'. The recent resolution of the structure of a major portion of the stator stalk of mitochondrial ATP synthase represents an important step towards a structural model for the ATP synthase holoenzyme.
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