Does F1‐ATPase subunit γ turn in the wrong direction?

FEBS Letters

Berzborn, Richard J.¹  Schlitter, Jürgen² 

[1] Department of Biochemistry of Plants, Ruhr-University Bochum, Biology, 44780 Bochum, Germany;Department of Biophysics, Ruhr-University Bochum, Biology, 44780 Bochum, Germany

关键词: ATP synthesis;    Rotation;    Coupling;    Hydrogen bond;    MEP;    most eccentric point;    Pi;    inorganic phosphate anion;    Amino acids are mostly given in the single letter code;    e.g. γM23K means a mutation of residue subunit γ methionine 23 to lysine;   

DOI  :  10.1016/S0014-5793(02)03735-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Analyzing the direction of F₁-ATPase subunit γ rotation, its shape and non-random distribution of surface residues, a mechanism is proposed for how γ induces the closing/opening of the catalytic sites at β/α interfaces: by keeping contact with the mobile domain of subunits β at the ‘jaw’ (D386, the seven consecutive hydrophobic residues and D394/E395), rotating γ works as a screw conveyer within the barrel of (α,β)₃. Mutations of the conveyer contacts are predicted to inhibit. Rotating wheel cartoons illustrate enzyme turnover and conformational changes. Steric clashes, polar interactions and also substrate limitations lead to specific stops. Because it is constructed as a stepper, γ prevents uncoupling at high energy charge.

【 授权许可】

Unknown