title: Rotary ATPases--dynamic molecular machines.
abstract: Recent work has provided the detailed overall architecture and subunit composition of three subtypes of rotary ATPases. Composite models of F-type, V-type and A-type ATPases have been constructed by fitting high-resolution X-ray structures of individual components into electron microscopy derived envelopes of the intact enzymes. Electron cryo-tomography has provided new insights into the supra-molecular arrangement of eukaryotic ATP synthases within mitochondria. An inherent flexibility in rotary ATPases observed by different techniques suggests greater dynamics during operation than previously envisioned. The concerted movement of subunits within the complex might provide means of regulation and information transfer between distant parts of rotary ATPases thereby fine tuning these molecular machines to their cellular environment, while optimizing their efficiency.
authors.affiliation: The Victor Chang Cardiac Research Institute, Sydney, NSW, Australia; The University of New South Wales, Sydney, NSW, Australia. Electronic address: a.stewart@victorchang.edu.au.
authors.forename: Alastair G
authors.initials: AG
authors.lastname: Stewart
authors.affiliation: The Victor Chang Cardiac Research Institute, Sydney, NSW, Australia; The University of New South Wales, Sydney, NSW, Australia.
authors.forename: Elise M
authors.initials: EM
authors.lastname: Laming
authors.affiliation: The Victor Chang Cardiac Research Institute, Sydney, NSW, Australia; The University of New South Wales, Sydney, NSW, Australia.
authors.forename: Meghna
authors.initials: M
authors.lastname: Sobti
authors.affiliation: The Victor Chang Cardiac Research Institute, Sydney, NSW, Australia; The University of New South Wales, Sydney, NSW, Australia.
authors.forename: Daniela
authors.initials: D
authors.lastname: Stock
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism*; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012399:Rotation
chemical_list: D020409:Molecular Motor Proteins; D000251:Adenosine Triphosphatases