Rotary ATPases--dynamic molecular machines

Alastair G Stewart; Elise M Laming; Meghna Sobti; Daniela Stock

doi:10.1016/j.sbi.2013.11.013

Rotary ATPases--dynamic molecular machines

Curr Opin Struct Biol. 2014 Apr:25:40-8. doi: 10.1016/j.sbi.2013.11.013. Epub 2013 Dec 21.

Authors

Alastair G Stewart¹, Elise M Laming², Meghna Sobti², Daniela Stock²

Affiliations

¹ 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.
² The Victor Chang Cardiac Research Institute, Sydney, NSW, Australia; The University of New South Wales, Sydney, NSW, Australia.

PMID: 24878343
DOI: 10.1016/j.sbi.2013.11.013

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.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Adenosine Triphosphatases / chemistry
Adenosine Triphosphatases / metabolism*
Molecular Motor Proteins / chemistry
Molecular Motor Proteins / metabolism*
Protein Multimerization
Protein Structure, Quaternary
Rotation*

Substances

Molecular Motor Proteins
Adenosine Triphosphatases