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Article

Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase.

The Journal of biological chemistry - 26 Jun 2009

Iino Ryota, Hasegawa Rie, Tabata Kazuhito V, Noji Hiroyuki

Abstract excerpt

The epsilon subunit of bacterial FoF1-ATP synthase (FoF1), a rotary motor protein, is known to inhibit the ATP hydrolysis reaction of this enzyme. The inhibitory effect is modulated by the conformation of the C-terminal alpha-helices of epsilon, and the "extended" but not "hairpin-folded" state is responsible for inhibition. Although the inhibition of ATP hydrolysis by the C-terminal domain of epsilon has been...

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Identifiers

PMID: 19411254
DOI: 10.1074/jbc.M109.003798
PMCID: PMC2719386

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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