5cdf

Publication Abstract from PubMed

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 alpha-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 zeta inhibitor protein, an alpha-helical protein that binds to the catalytic F1 domain of the enzyme. This domain is a complex of three alpha-subunits and three beta-subunits, and one copy of each of the gamma-, delta- and -subunits. Attempts to crystallize the F1-zeta inhibitor complex yielded crystals of a subcomplex of the catalytic domain containing the alpha- and beta-subunits only. Its structure was determined to 2.3 A resolution and consists of a heterodimer of one alpha-subunit and one beta-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.

Structure of a catalytic dimer of the alpha- and beta-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 A resolution.,Morales-Rios E, Montgomery MG, Leslie AG, Garcia-Trejo JJ, Walker JE Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1309-17. doi:, 10.1107/S2053230X15016076. Epub 2015 Sep 23. PMID:26457523^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.