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Dynamic mechanisms driving conformational conversions of the ? and ? subunits involved in rotational catalysis of F1-ATPase.

ABSTRACT: F-type ATPase is a ubiquitous molecular motor. Investigations on thermophilic F1-ATPase and its subunits, ? and ?, by NMR were reviewed. Using specific isotope labeling, pKa of the putative catalytic carboxylate in ? was estimated. Segmental isotope-labeling enabled us to monitor most residues of ?, revealing that the conformational conversion from open to closed form of ? on nucleotide binding found in ATPase was an intrinsic property of ? and could work as a driving force of the rotational catalysis. A stepwise conformational change was driven by switching of the hydrogen bond networks involving Walker A and B motifs. Segmentally labeled ATPase provided a well resolved NMR spectra, revealing while the open form of ? was identical for ? monomer and ATPase, its closed form could be different. ATP-binding was also a critical factor in the conformational conversion of ?, an ATP hydrolysis inhibitor. Its structural elucidation was described.

SUBMITTER: Akutsu H 

PROVIDER: S-EPMC5743862 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of F<sub>1</sub>-ATPase.

Akutsu Hideo H  

Proceedings of the Japan Academy. Series B, Physical and biological sciences 20170101 8

F-type ATPase is a ubiquitous molecular motor. Investigations on thermophilic F<sub>1</sub>-ATPase and its subunits, β and ε, by NMR were reviewed. Using specific isotope labeling, pK<sub>a</sub> of the putative catalytic carboxylate in β was estimated. Segmental isotope-labeling enabled us to monitor most residues of β, revealing that the conformational conversion from open to closed form of β on nucleotide binding found in ATPase was an intrinsic property of β and could work as a driving force  ...[more]

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