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ATP‐driven rotation of the γ subunit in F 1 ‐ATPase
Author(s) -
Weber Joachim,
Nadanaciva Sashi,
Senior Alan E
Publication year - 2000
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(00)02071-8
Subject(s) - gamma subunit , atpase , atp hydrolysis , chemistry , protein subunit , crystallography , rotation (mathematics) , hydrolysis , phosphate , stereochemistry , alpha (finance) , biophysics , conformational change , enzyme , biochemistry , biology , medicine , construct validity , geometry , mathematics , nursing , patient satisfaction , gene
We present a mechanism for F 1 ‐ATPase in which hydrolysis of MgATP in the high‐affinity catalytic site at the α/β interface drives rotation of the γ subunit via conformational changes in the α subunit. During hydrolysis, transition state formation and separation of P i from MgADP causes movement of portions of α, transmitted via two Arg residues which are hydrogen‐bonded to the γ‐phosphate of MgATP, αArg376 and βArg182; the latter is also hydrogen‐bonded to interfacial α residues between α346 and α349. Changes in α conformation then push on γ, resulting in rotation. Supporting evidence from the literature and from new data is discussed.