1chr
From Proteopedia
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CRYSTAL STRUCTURE OF CHLOROMUCONATE CYCLOISOMERASE FROM ALCALIGENES EUTROPHUS JMP134 (PJP4) AT 3 ANGSTROMS RESOLUTION
Overview
Chloromuconate cycloisomerase (E.C. 5.5.1.7) is an enzyme involved in the, 2,4-dichlorophenoxyacetate degradation pathway of Alcaligenes eutrophus, JMP134 (pJP4). The crystal structure of this protein was determined at 3 A, resolution by molecular-replacement techniques using atomic coordinates, from the reported crystal structure of the homologous muconate, cycloisomerase (E.C. 5.5.1.1) from Pseudomonas putida as the search model, (42% identical positions in the sequences). Structure refinement by, simulated-annealing and restrained least-squares techniques converged at R, = 0.195. In the crystals studied, space group I4, the protein is present, as two octamers per unit cell with two subunits per asymmetric unit. Each, subunit consists of two globular domains, one of which forms an, alpha/beta-barrel. Comparison of this structure with that of muconate, cycloisomerase reveals the reasons for the altered substrate specificity, of chloromuconate cycloisomerase. Marked differences are observed in, polarity, accessibility and hydrogen-bonding potential in the channel, leading into the active site as well as in the active center itself.
About this Structure
1CHR is a Single protein structure of sequence from Cupriavidus necator with MN and CL as ligands. Active as Chloromuconate cycloisomerase, with EC number 5.5.1.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of chloromuconate cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4) at 3 A resolution., Hoier H, Schlomann M, Hammer A, Glusker JP, Carrell HL, Goldman A, Stezowski JJ, Heinemann U, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):75-84. PMID:15299479
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