ATP synthase - the structure of the stator stalk

Research output: Contribution to journalShort surveypeer-review

34 Scopus citations


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 languageEnglish
Pages (from-to)53-56
Number of pages4
JournalTrends in Biochemical Sciences
Issue number2
StatePublished - Feb 2007


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