Document Type

Article

Publication Date

6-1-2011

Comments

This article has been peer reviewed. It was published in: Nature structural and molecular biology

Volume 18, Issue 6, June 2011, Pages 701-7.

The published version is available at DOI: 10.1038/nsmb.2058. Copyright © MacMillan Science Communication.

Abstract

ATP synthase is a membrane-bound rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, autoinhibition by one of its rotary stalk subunits occurs in bacteria and chloroplasts but not in mitochondria. The crystal structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli described here reveals the structural basis for this inhibition. The C-terminal domain of subunit ɛ adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme and engages both rotor and stator subunits in extensive contacts that are incompatible with functional rotation. As a result, the three catalytic subunits are stabilized in a set of conformations and rotational positions distinct from previous F(1) structures.

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