FEBS Letters | |
ATP‐driven rotation of the γ subunit in F1‐ATPase | |
Nadanaciva, Sashi1  Senior, Alan E1  Weber, Joachim1  | |
[1] Department of Biochemistry and Biophysics, Box 712, University of Rochester Medical Center, Rochester, NY 14642, USA | |
关键词: ATP synthase; ATP synthesis; ATP hydrolysis; Rotation; Nucleotide binding; | |
DOI : 10.1016/S0014-5793(00)02071-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
We present a mechanism for F1-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 Pi 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.
【 授权许可】
Unknown
【 预 览 】
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