1s9r
From Proteopedia
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CRYSTAL STRUCTURE OF ARGININE DEIMINASE COVALENTLY LINKED WITH A REACTION INTERMEDIATE
Overview
Arginine deiminase (ADI), an enzyme that hydrolyzes arginine to generate, energy in many parasitic microorganisms, has potent anticancer activities, and can halt growth of solid tumors. We determined the crystal structure, of ADI from Mycoplasma arginini in two different forms (1.6 and 2.0 A, resolution) using multiple isomorphous replacement. ADI shares common, structural features with the arginine-catabolizing enzymes Arg:Gly, amidinotransferase and dimethylarginine dimethyl-aminohydrolase; ADI, contains an additional domain of five helices. The scissile C-N bonds of, the substrates and the catalytic triads (Cys398-His269-Glu213 of ADI) for, the three enzymes superimpose on each other. The ADI structure from form I, crystals corresponds to a tetrahedral intermediate with four heteroatoms, (1S, 2N, 1O) covalently bonded to the reaction-center carbon. The, structure from form II crystals represents an amidino-enzyme complex; the, reaction-center carbon is covalently bonded to Cys398 sulfur and two, nitrogens, and the reacting water molecule is only 2.54 A away.
About this Structure
1S9R is a Single protein structure of sequence from Mycoplasma arginini with ARG, TRS and UNX as ligands. Active as Arginine deiminase, with EC number 3.5.3.6 Full crystallographic information is available from OCA.
Reference
Crystal structures of arginine deiminase with covalent reaction intermediates; implications for catalytic mechanism., Das K, Butler GH, Kwiatkowski V, Clark AD Jr, Yadav P, Arnold E, Structure. 2004 Apr;12(4):657-67. PMID:15062088
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