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Bioarchitecture. 2013 Jan-Feb;3(1):2-12. doi: 10.4161/bioa.23301. Epub 2013 Jan 1.

Rotary ATPases: models, machine elements and technical specifications.

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The Victor Chang Cardiac Research Institute, Faculty of Medicine, The University of New South Wales, Sydney, NSW, Australia.


Rotary ATPases are molecular rotary motors involved in biological energy conversion. They either synthesize or hydrolyze the universal biological energy carrier adenosine triphosphate. Recent work has elucidated the general architecture and subunit compositions of all three sub-types of rotary ATPases. Composite models of the intact F-, V- and A-type ATPases have been constructed by fitting high-resolution X-ray structures of individual subunits or sub-complexes into low-resolution electron densities of the intact enzymes derived from electron cryo-microscopy. Electron cryo-tomography has provided new insights into the supra-molecular arrangement of eukaryotic ATP synthases within mitochondria and mass-spectrometry has started to identify specifically bound lipids presumed to be essential for function. Taken together these molecular snapshots show that nano-scale rotary engines have much in common with basic design principles of man made machines from the function of individual "machine elements" to the requirement of the right "fuel" and "oil" for different types of motors.


A-type ATPase; ATP synthase; X-ray crystallography; biological motors; electron microscopy; energy conversion; rotary motors; structural biology; vacuolar ATPase

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