| Literature DB >> 17208001 |
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.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17208001 PMCID: PMC2570231 DOI: 10.1016/j.tibs.2006.12.006
Source DB: PubMed Journal: Trends Biochem Sci ISSN: 0968-0004 Impact factor: 13.807