ATP synthase - the structure of the stator stalk

Research output: Contribution to journalShort survey

31 Scopus citations

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 languageEnglish
Pages (from-to)53-56
Number of pages4
JournalTrends in Biochemical Sciences
Volume32
Issue number2
DOIs
StatePublished - Feb 2007

Fingerprint Dive into the research topics of 'ATP synthase - the structure of the stator stalk'. Together they form a unique fingerprint.

  • Cite this