2oal | pdb_00002oal

RebH with bound FAD

spinqualitylabelsall models 2oal, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2oal is a 2 chain structure with sequence from "nocardia_aerocolonigenes"_(shinobu_and_kawato_1960)_pridham_1970 "nocardia aerocolonigenes" (shinobu and kawato 1960) pridham 1970. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FAD Related: 2e4g, 2oam Gene: rbmJ, rebH ("Nocardia aerocolonigenes" (Shinobu and Kawato 1960) Pridham 1970) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [REBH_NOCAE] Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyze the chlorination of tryptophan (Trp) at C7 position to yield 7-chlorotryptophan. The reaction between FADH2, Cl-, and O2 generates the powerful oxidant HOCl, which is presumed to carry out the chlorination reaction. The reaction of HOCl with the active site Lys-79 generates a lysine chloramine, which plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. It is also able to use bromide ions to generate monobrominated Trp. 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 flavin-dependent halogenase RebH catalyzes the formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin. The reaction of FADH2, Cl-, and O2 in the active site generates the powerful oxidant HOCl, which was presumed to carry out the chlorination reaction. Herein, we demonstrate the formation of a long-lived chlorinating intermediate (t1/2 = 63 h at 4 degrees C) when RebH, FADH2, Cl-, and O2 react in the absence of substrate tryptophan. This intermediate remained on the enzyme after removal of FAD and transferred chlorine to tryptophan with kinetically competent rates. The identity of this intermediate is suggested by the X-ray crystal structure of RebH, which revealed an active site Lys79 located in a central position between flavin and tryptophan binding sites and just 4.1 A above C7 of tryptophan. The chlorinating species is proposed to be a Lys-epsilonNH-Cl (lysine chloramine) from reaction of enzyme-generated HOCl with the active site Lys79. This covalent enzyme chloramine likely plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases.,Yeh E, Blasiak LC, Koglin A, Drennan CL, Walsh CT Biochemistry. 2007 Feb 6;46(5):1284-92. PMID:17260957 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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