1brt | pdb_00001brt

BROMOPEROXIDASE A2 MUTANT M99T

spinqualitylabelsall models 1brt, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1brt is a 1 chain structure with sequence from Atcc 10762. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL Gene: BPOA2 (ATCC 10762) Activity: Chloride peroxidase, with EC number 1.11.1.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BPOA2_STRAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. 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 structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites. Structural investigation of the cofactor-free chloroperoxidases.,Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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