1d6u

CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE

spinqualitylabelsall models 1d6u, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1d6u is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CU, GOL, HY1, PEA NonStd Res: TYQ Related: 1oac, 1spu, 1jez, 1qaf, 1qak, 1qal, 1d6y, 1d6z Activity: Oxidoreductase, with EC number and 1.4.3.22 1.4.3.21 and 1.4.3.22 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 X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal. Visualization of dioxygen bound to copper during enzyme catalysis.,Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE Science. 1999 Nov 26;286(5445):1724-8. PMID:10576737 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Copper Amine Oxidase

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