Molecular Switch of F0F1-ATP Synthase, G-protein, and Other ATP-driven Enzymes

Overview

Journal J Bioenerg Biomembr

Publisher Springer

Specialties Biochemistry
Biology
Endocrinology

Date 1996 Oct 1

PMID 8951093

Citations 1

Authors

H Noji

T Amano

M Yoshida

Affiliations

Soon will be listed here.

Abstract

Exchange-out of amide tritium from labeled gamma-subunit of alpha 3 beta 3 gamma complex of F0F1-ATP synthase was not accelerated by ATP, suggesting that hemagglutinin-type transition of coiled-coil structure did not occur in gamma-subunit. Local topology of nucleotide binding site and "switch II" region of G-protein alpha resemble those of F1-beta subunit and other proteins which catalyze ATP-triggered reactions. Probably, binding of nucleotide to F0F1-ATP synthase induces conformational change of the switch II-like region with transforming beta subunit structure from "open" to "close" for and this transformation results in loss of hydrogen bonds with gamma subunit, thus enabling the gamma subunit to move.

Citing Articles

The alpha/beta interfaces of alpha(1)beta(1), alpha(3)beta(3), and F1: domain motions and elastic energy stored during gamma rotation.

Kagawa Y, Hamamoto T, Endo H J Bioenerg Biomembr. 2004; 32(5):471-84.

PMID: 15254382 DOI: 10.1023/a:1005612923995.

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