| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2031397 | Trends in Biochemical Sciences | 2007 | 4 Pages |
Abstract
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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Authors
Joachim Weber,