2CK3

Azide inhibited bovine F1-ATPase

Summary for 2CK3

• Entry DOI: 10.2210/pdb2ck3/pdb
• Related: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1H8H 1NBM 1OHH 1QO1 1W0J 1W0K
• Descriptor: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, PHOSPHATE ION, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ... (11 entities in total)
• Functional Keywords: hydrolase
• Biological source: BOS TAURUS (BOVINE); More
• Cellular location: Mitochondrion inner membrane (By similarity): P19483; Mitochondrion: P00829 P05631 P05630 P05632
• Total number of polymer chains: 9
• Total formula weight: 374810.81

Authors

Bowler, M.W.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2006-04-10, release date: 2006-05-08, Last modification date: 2023-12-13)

Primary citation

Bowler, M.W.,Montgomery, M.G.,Leslie, A.G.,Walker, J.E.
How Azide Inhibits ATP Hydrolysis by the F-Atpases.
Proc.Natl.Acad.Sci.USA, 103:8646-, 2006

PubMed Abstract: In the structure of bovine F1-ATPase determined at 1.95-A resolution with crystals grown in the presence of ADP, 5'-adenylyl-imidodiphosphate, and azide, the azide anion interacts with the beta-phosphate of ADP and with residues in the ADP-binding catalytic subunit, betaDP. It occupies a position between the catalytically essential amino acids, beta-Lys-162 in the P loop and the "arginine finger" residue, alpha-Arg-373, similar to the site occupied by the gamma-phosphate in the ATP-binding subunit, betaTP. Its presence in the betaDP-subunit tightens the binding of the side chains to the nucleotide, enhancing its affinity and thereby stabilizing the state with bound ADP. This mechanism of inhibition appears to be common to many other ATPases, including ABC transporters, SecA, and DNA topoisomerase IIalpha. It also explains the stimulatory effect of azide on ATP-sensitive potassium channels by enhancing the binding of ADP.

PubMed: 16728506
DOI: 10.1073/PNAS.0602915103

Experimental method

X-RAY DIFFRACTION (1.95 Å)