Premium
Regulation of the F 0 F 1 ‐ATP synthase: The conformation of subunit ε might be determined by directionality of subunit γ rotation
Author(s) -
Feniouk Boris A.,
Junge Wolfgang
Publication year - 2005
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/j.febslet.2005.08.030
Subject(s) - atp synthase gamma subunit , protein subunit , atp synthase , atp hydrolysis , directionality , chemistry , biophysics , stereochemistry , conformational change , atpase , enzyme , biochemistry , biology , microbiology and biotechnology , gene
We propose that the directionality of the coiled‐coil subunit γ rotation determines whether subunit ε is in contracted or extended form. Block of rotation by MgADP presumably induces the extended conformation of subunit ε. This conformation might serve as a safety lock, stabilizing the ADP‐inhibited state upon de‐energization and preventing spontaneous re‐activation and wasteful ATP hydrolysis. The hypothesis merges the known regulatory effects of ADP, protonmotive force and conformational changes of subunit ε into a consistent picture.