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Article

Stepwise propagation of the ATP-induced conformational change of the F1-ATPase beta subunit revealed by NMR.

The Journal of biological chemistry - 23 Jan 2009

Yagi Hiromasa, Kajiwara Nobumoto, Iwabuchi Tomoyuki, Izumi Kenya, Yoshida Masasuke, Akutsu Hideo

Abstract excerpt

The rotation of F1-ATPase (F1) is driven by the open/close bending motion of the beta subunit. The mechanism underlying the bending motion was investigated for the F1beta monomer from thermophilic Bacillus PS3 (TF1beta) in solution, using mutagenesis and NMR. The hydrogen bond networks involving the side chains of Lys-164 (numbering for TF1beta; 162 for mitochondrial F1beta in parentheses), Thr-165(163),...

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Identifiers

PMID: 19028677
DOI: 10.1074/jbc.M808212200

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