Rotary ATPases—dynamic molecular machines

• Published in: Current opinion in structural biology 2014-04, Vol.25, p.40-48
• Main Authors: Stewart, Alastair G, Laming, Elise M, Sobti, Meghna, Stock, Daniela
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; Molecular Motor Proteins - chemistry; Molecular Motor Proteins - metabolism; Protein Multimerization; Protein Structure, Quaternary; Rotation
• ISSN: 0959-440X; 1879-033X
• DOI: 10.1016/j.sbi.2013.11.013

•Visualization of rotary ATPases on nanometre scale by cryo-electron microscopy.•In situ visualization of mitochondrial ATP synthase by electron cryo-tomography.•Functional implications of peripheral stalk structures and wobble theory. 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.