Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution.
Acta Crystallographica Section F: Structural Biology Communications
International Union of Crystallography
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Morales-Ríos, E., Montgomery, M., Leslie, A., García-Trejo, J., & Walker, J. (2015). Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution.. Acta Crystallographica Section F: Structural Biology Communications, 71 (10), 1309-1317. https://doi.org/10.1107/S2053230X15016076
The structures of F-ATPases have predominantly been determined from mitochondrial enzymes, and those of the enzymes in eubacteria have been less studied. Paracoccus denitrificans is a member of the α-proteobacteria and is related to the extinct protomitochondrion that became engulfed by the ancestor of eukaryotic cells. The P. denitrificans F-ATPase is an example of a eubacterial F-ATPase that can carry out ATP synthesis only, whereas many others can catalyse both the synthesis and the hydrolysis of ATP. Inhibition of the ATP hydrolytic activity of the P. denitrificans F-ATPase involves the ζ inhibitor protein, an α-helical protein that binds to the catalytic F1 domain of the enzyme. This domain is a complex of three α-subunits and three β-subunits, and one copy of each of the γ-, δ- and ℇ-subunits. Attempts to crystallize the F1-ζ inhibitor complex yielded crystals of a subcomplex of the catalytic domain containing the α- and β-subunits only. Its structure was determined to 2.3 Å resolution and consists of a heterodimer of one α-subunit and one β-subunit. It has no bound nucleotides, and it corresponds to the `open' or `empty' catalytic interface found in other F-ATPases. The main significance of this structure is that it aids in the determination of the structure of the intact membrane-bound F-ATPase, which has been crystallized.
F-ATPase, Paracoccus denitrificans, catalytic αβ dimer, structure, α-proteobacteria, Bacterial Proteins, Biocatalysis, Crystallization, Crystallography, X-Ray, Paracoccus denitrificans, Protein Multimerization, Protein Subunits, Proton-Translocating ATPases
This work was funded by the intra-mural program of the Medical Research Council via MRC program U105663150 to J. E. W., and additionally E. M.-R. was supported partially by Consejo Nacional de Ciencia y Tecnología as part of the program ‘Estancias Posdoctorales y Sabáticas en el Extranjero para la Consolidación de Grupos de Investigación’ grant 175676. A. G. W. L. was supported by MRC program U105184325. J.J.G.-T. was supported by grant CB-2011-01-167622 from the Consejo Nacional de Ciencia y Tecnología de México, and grant PAPIIT-IN211012 from the Dirección General de Asuntos del Personal Académico of U.N.A.M.
External DOI: https://doi.org/10.1107/S2053230X15016076
This record's URL: https://www.repository.cam.ac.uk/handle/1810/266071