Structural basis of unisite catalysis of bacterial F0F1-ATPase. Issue 3 (11th July 2022)

• Record Type: Journal Article
• Authors: Nakano, Atsuki; Kishikawa, Jun-ichi; Nakanishi, Atsuko; Mitsuoka, Kaoru; Yokoyama, Ken
• Editors: Yooseph, Shibu
• Is Part Of: PNAS nexus. Volume 1:Issue 3(2022)
• Publication Date: 2022-07-11
• Subjects: Science -- Periodicals; 505
• DOI: 10.1093/pnasnexus/pgac116
• Languages: English
• ISSNs: 2752-6542

Abstract

Abstract: Adenosine triphosphate (ATP) synthases (F0 F1 -ATPases) are crucial for all aerobic organisms. F1, a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the central γε rotor inside a cylinder made of α 3 β 3 in three different conformations (referred to as β E, β TP, and β DP ). In this study, we determined multiple cryo-electron microscopy structures of bacterial F0 F1 exposed to different reaction conditions. The structures of nucleotide-depleted F0 F1 indicate that the ε subunit directly forces β TP to adopt a closed form independent of the nucleotide binding to β TP . The structure of F0 F1 under conditions that permit only a single catalytic β subunit per enzyme to bind ATP is referred to as unisite catalysis and reveals that ATP hydrolysis unexpectedly occurs on β TP instead of β DP, where ATP hydrolysis proceeds in the steady-state catalysis of F0 F1 . This indicates that the unisite catalysis of bacterial F0 F1 significantly differs from the kinetics of steady-state turnover with continuous rotation of the shaft.