title: ATP synthase--the structure of the stator stalk.
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.
authors.affiliation: Department of Chemistry and Biochemistry, Texas Tech University, Box 41061, Lubbock, TX 79409-1061, USA. joachim.weber@ttuhsc.edu
authors.forename: Joachim
authors.initials: J
authors.lastname: Weber
mesh_terms: D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D025261:Mitochondrial Proton-Translocating ATPases