2ck3

Azide inhibited bovine F1-ATPaseAzide inhibited bovine F1-ATPase

Structural highlights 2ck3 is a 9 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , , Related: 1e79, 1h8e, 1bmf, 1cow, 1e1q, 1e1r, 1efr, 1h8h, 1nbm, 1ohh, 1qo1, 1w0j, 1w0k Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. How azide inhibits ATP hydrolysis by the F-ATPases.,Bowler MW, Montgomery MG, Leslie AG, Walker JE Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8646-9. Epub 2006 May 25. PMID:16728506 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase

spinqualitylabelsall models 2ck3, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image