Mechanism of the conformational change of the F1-ATPase β subunit revealed by free energy simulations

Yuko Ito, Tomotaka Oroguchi, Mitsunori Ikeguchi

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)

Abstract

F1-ATPase is an ATP-driven rotary motor enzyme. The β subunit changes its conformation from an open to a closed form upon ATP binding. The motion in the β subunit is regarded as a major driving force for rotation of the central stalk. In this Article, we explore the conformational change of the β subunit using all-atom free energy simulations with explicit solvent and propose a detailed mechanism for the conformational change. The β subunit conformational change is accomplished roughly in two characteristic steps: changing of the hydrogen-bond network around ATP and the dynamic movement of the C-terminal domain via sliding of the B-helix. The details of the former step agree well with experimental data. In the latter step, sliding of the B-helix enhances the hydrophobic stabilization due to the exclusion of water molecules from the interface and improved packing in the hydrophobic core. This step contributes to a decrease in free energy, leading to the generation of torque in the F1-ATPase upon ATP binding.

Original languageEnglish
Pages (from-to)3372-3380
Number of pages9
JournalJournal of the American Chemical Society
Volume133
Issue number10
DOIs
Publication statusPublished - 2011 Mar 16
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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