ATP-driven rotation of the γ subunit in F1-ATPase

Joachim Weber, Sashi Nadanaciva, Alan E. Senior

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


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 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. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)1-5
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - Oct 13 2000


  • ATP hydrolysis
  • ATP synthase
  • ATP synthesis
  • Nucleotide binding
  • Rotation


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