2wpd | pdb_00002wpd

THE MG.ADP INHIBITED STATE OF THE YEAST F1C10 ATP SYNTHASE

spinqualitylabelsall models 2wpd, resolution 3.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wpd is a 19 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, ATP, MG 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 The F(1)c(10) subcomplex of the yeast F(1)F(0)-ATP synthase includes the membrane rotor part c(10)-ring linked to a catalytic head, (alphabeta)(3), by a central stalk, gammadeltaepsilon. The Saccharomyces cerevisiae yF(1)c(10).ADP subcomplex was crystallized in the presence of Mg.ADP, dicyclohexylcarbodiimide (DCCD), and azide. The structure was solved by molecular replacement using a high resolution model of the yeast F(1) and a bacterial c-ring model with 10 copies of the c-subunit. The structure refined to 3.43-A resolution displays new features compared with the original yF(1)c(10) and with the yF(1) inhibited by adenylyl imidodiphosphate (AMP-PNP) (yF(1)(I-III)). An ADP molecule was bound in both beta(DP) and beta(TP) catalytic sites. The alpha(DP)-beta(DP) pair is slightly open and resembles the novel conformation identified in yF(1), whereas the alpha(TP)-beta(TP) pair is very closed and resembles more a DP pair. yF(1)c(10).ADP provides a model of a new Mg.ADP-inhibited state of the yeast F(1). As for the original yF(1) and yF(1)c(10) structures, the foot of the central stalk is rotated by approximately 40 degrees with respect to bovine structures. The assembly of the F(1) central stalk with the F(0) c-ring rotor is mainly provided by electrostatic interactions. On the rotor ring, the essential cGlu(59) carboxylate group is surrounded by hydrophobic residues and is not involved in hydrogen bonding. Crystal structure of the Mg.ADP-inhibited state of the yeast F1c10-ATP synthase.,Dautant A, Velours J, Giraud MF J Biol Chem. 2010 Sep 17;285(38):29502-10. Epub 2010 Jul 7. PMID:20610387 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase

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