Effects of mutations in the beta subunit hinge domain on ATP synthase F1 sector rotation: interaction between Ser 174 and Ile 163.

doi:10.1016/j.bbrc.2007.10.157

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Article

Effects of mutations in the beta subunit hinge domain on ATP synthase F1 sector rotation: interaction between Ser 174 and Ile 163.

Biochemical and biophysical research communications - 11 Jan 2008

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

Abstract excerpt

A complex of gamma, epsilon, and c subunits rotates in ATP synthase (F(o)F(1)) coupling with proton transport. Replacement of betaSer174 by Phe in beta-sheet4 of the beta subunit (betaS174F) caused slow gamma subunit revolution of the F(1) sector, consistent with the decreased ATPase activity [M. Nakanishi-Matsui, S. Kashiwagi, T. Ubukata, A. Iwamoto-Kihara, Y. Wada, M. Futai, Rotational catalysis of Escherichia...

Topics

Molecular Motor Proteins
Mutagenesis, Site-Directed
Mutation
Protein Subunits
Proton-Translocating ATPases
Rotation
Structure-Activity Relationship

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Identifiers

PMID: 17983592
DOI: 10.1016/j.bbrc.2007.10.157

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