1e79 | pdb_00001e79

Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide)

spinqualitylabelsall models 1e79, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1e79 is a 9 chain structure with sequence from Bos taurus. The December 2005 RCSB PDB Molecule of the Month feature on ATP Synthase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, ATP, DCW, GOL, MG, SO4 Related: 1bmf, 1cow, 1e1q, 1e1r, 1efr, 1nbm, 1qo1 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 central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The gamma subunit penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. In other crystals of F(1)-ATPase, the protrusion was disordered, but with crystals of F(1)-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (alpha beta)(3) domain. The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.,Gibbons C, Montgomery MG, Leslie AG, Walker JE Nat Struct Biol. 2000 Nov;7(11):1055-61. PMID:11062563 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also A-ATP Synthase ATPase

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