7XKH

Nucleotide-depleted F1 domain of FoF1-ATPase from Bacillus PS3, state1

Summary for 7XKH

• Entry DOI: 10.2210/pdb7xkh/pdb
• EMDB information: 33251
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (5 entities in total)
• Functional Keywords: atp synthase f1 atpase fof1, motor protein
• Biological source: Bacillus sp. PS3; More
• Total number of polymer chains: 8
• Total formula weight: 371361.08

Authors

Nakano, A.,Kishikawa, J.,Nakanishi, A.,Mitsuoka, K.,Yokoyama, K. (deposition date: 2022-04-19, release date: 2022-09-21, Last modification date: 2023-10-11)

Primary citation

Nakano, A.,Kishikawa, J.I.,Nakanishi, A.,Mitsuoka, K.,Yokoyama, K.
Structural basis of unisite catalysis of bacterial F 0 F 1 -ATPase.
Pnas Nexus, 1:pgac116-pgac116, 2022

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

PubMed: 36741449
DOI: 10.1093/pnasnexus/pgac116

Experimental method

ELECTRON MICROSCOPY (3.1 Å)