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.
Original language | English |
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Pages (from-to) | 53-56 |
Number of pages | 4 |
Journal | Trends in Biochemical Sciences |
Volume | 32 |
Issue number | 2 |
DOIs | |
State | Published - Feb 2007 |