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The structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF₁.

Published version
Peer-reviewed

Type

Article

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Authors

Robinson, Graham C 
Bason, John V 
Montgomery, Martin G 
Fearnley, Ian M 
Mueller, David M 

Abstract

The structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF₁ has been determined at 2.5 Å resolution. The inhibitory region of IF₁ from residues 1 to 36 is entrapped between the C-terminal domains of the α(DP)- and β(DP)-subunits in one of the three catalytic interfaces of the enzyme. Although the structure of the inhibited complex is similar to that of the bovine-inhibited complex, there are significant differences between the structures of the inhibitors and their detailed interactions with F₁-ATPase. However, the most significant difference is in the nucleotide occupancy of the catalytic β(E)-subunits. The nucleotide binding site in β(E)-subunit in the yeast complex contains an ADP molecule without an accompanying magnesium ion, whereas it is unoccupied in the bovine complex. Thus, the structure provides further evidence of sequential product release, with the phosphate and the magnesium ion released before the ADP molecule.

Description

Keywords

Adenosine Diphosphate, Animals, Binding Sites, Catalysis, Catalytic Domain, Cattle, Crystallography, X-Ray, Hydrolysis, Protein Binding, Protein Conformation, Proteins, Proton-Translocating ATPases, Saccharomyces cerevisiae

Journal Title

Open Biology

Conference Name

Journal ISSN

2046-2441
2046-2441

Volume Title

3

Publisher

The Royal Society
Sponsorship
Medical Research Council (MC_U105663150)
Support for this work was provided by the Medical Research Council, UK, including a PhD studentship (to G.C.R.) and a Career Training Fellowship (to J.V.B.), by the European Drug Initiative in Channels and Transporters (EDICT; to J.E.W.), and by a grant from NIH no. R01GM66223 to D.M.M.