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Does F 1 ‐ATPase subunit γ turn in the wrong direction?
Author(s) -
Berzborn Richard J.,
Schlitter Jürgen
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03735-3
Subject(s) - turn (biochemistry) , protein subunit , steric effects , biophysics , beta (programming language) , chemistry , rotation (mathematics) , substrate (aquarium) , atpase , gamma subunit , conformational change , mechanism (biology) , crystallography , stereochemistry , physics , enzyme , geometry , biochemistry , biology , computer science , mathematics , quantum mechanics , ecology , gene , programming language
Analyzing the direction of F 1 ‐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.