5CDF

Structure at 2.3 A of the alpha/beta monomer of the F-ATPase from Paracoccus denitrificans

Summary for 5CDF

• Entry DOI: 10.2210/pdb5cdf/pdb
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, GLYCEROL, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: Paracoccus denitrificans; More
• Cellular location: Cell inner membrane ; Peripheral membrane protein : A1B8N8 A1B8P0
• Total number of polymer chains: 2
• Total formula weight: 106317.49

Authors

Morales-Rios, E.,Montgomery, M.G.,Leslie, A.G.W.,Garcia-Trejo, J.J.,Walker, J.E. (deposition date: 2015-07-03, release date: 2015-10-07, Last modification date: 2024-01-10)

Primary citation

Morales-Rios, E.,Montgomery, M.G.,Leslie, A.G.,Garcia-Trejo, J.J.,Walker, J.E.
Structure of a catalytic dimer of the alpha- and beta-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 angstrom resolution.
Acta Crystallogr.,Sect.F, 71:1309-1317, 2015

PubMed Abstract: 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.

PubMed: 26457523
DOI: 10.1107/S2053230X15016076

Experimental method

X-RAY DIFFRACTION (2.3 Å)