7cyx

Crystal strcuture of Glycine oxidase from Bacillus cereus ATCC 14579

spinqualitylabelsall models 7cyx, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7cyx is a 2 chain structure with sequence from Bacillus cereus ATCC 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.41Å Ligands: FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q81HQ7_BACCR Publication Abstract from PubMed Glycine oxidase (GO) is an enzyme that catalyzes the oxidation of the primary and secondary amines of various chemicals, including glycine, and the enzyme has been applied in a variety of fields, such as biosensor and genetically modified glyphosate resistance plants. Here, we report that the gene product of BC0747 from Bacillus cereus (BcGO) shows oxidase activity for glycine and small d-amino acids, such as d-proline and d-alanine. We also determined the crystal structure of BcGO complexed with the FAD cofactor at a 2.36 A resolution and revealed how the cofactor binds to the deep pocket of the enzyme. We performed the molecular docking calculation of the glycine substrate to the BcGO structure and identified how the carboxyl- and amine-groups of the d-amino acid are stabilized at the substrate binding site. Structural analysis of BcGO also provided information on the structural basis for the stereospecificity of the enzyme to d-amino acids. In addition, we placed the glyphosate molecule, a plant herbicide, at the substrate binding site, and explained how the mutation of Gly51 to arginine enhances enzyme activity. Structural basis for stereospecificity to d-amino acid of glycine oxidase from Bacillus cereus ATCC 14579.,Seok J, Kim YJ, Kim IK, Kim KJ Biochem Biophys Res Commun. 2020 Sep 26. pii: S0006-291X(20)31846-5. doi:, 10.1016/j.bbrc.2020.09.093. PMID:32993959 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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