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Article

Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation.

Biochemical and biophysical research communications - 30 Apr 2010

Nakanishi-Matsui Mayumi, Kashiwagi Sachiko, Kojima Masaki, Nonaka Takamasa, Futai Masamitsu

Abstract excerpt

The ATP synthase beta subunit hinge domain (betaPhe148 approximately betaGly186, P-loop/alpha-helixB/loop/beta-sheet4, Escherichia coli residue numbering) dramatically changes in conformation upon nucleotide binding. We previously reported that F(1) with the betaSer174 to Phe mutation in the domain lowered the gamma subunit rotation speed, and thus decreased the ATPase activity [M. Nakanishi-Matsui, S. Kashiwagi,...

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Identifiers

PMID: 20331967
DOI: 10.1016/j.bbrc.2010.03.127

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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