2gjl
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Revision as of 18:01, 29 January 2008
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Crystal Structure of 2-nitropropane dioxygenase
Overview
Nitroalkane compounds are widely used in chemical industry and are also, produced by microorganisms and plants. Some nitroalkanes have been, demonstrated to be carcinogenic, and enzymatic oxidation of nitroalkanes, is of considerable interest. 2-Nitropropane dioxygenases from Neurospora, crassa and Williopsis mrakii (Hansenula mrakii), members of one family of, the nitroalkane-oxidizing enzymes, contain FMN and FAD, respectively. The, enzymatic oxidation of nitroalkanes by 2-nitropropane dioxygenase operates, by an oxidase-style catalytic mechanism, which was recently shown to, involve the formation of an anionic flavin semiquinone. This represents a, unique case in which an anionic flavin semiquinone has been experimentally, observed in the catalytic pathway for oxidation catalyzed by a, flavin-dependent enzyme. Here we report the first crystal structure of, 2-nitropropane dioxygenase from Pseudomonas aeruginosa in two forms: a, binary complex with FMN and a ternary complex with both FMN and, 2-nitropropane. The structure identifies His(152) as the proposed, catalytic base, thus providing a structural framework for a better, understanding of the catalytic mechanism.
About this Structure
2GJL is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Active as 2-nitropropane dioxygenase, with EC number 1.13.11.32 Full crystallographic information is available from OCA.
Reference
Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base., Ha JY, Min JY, Lee SK, Kim HS, Kim do J, Kim KH, Lee HH, Kim HK, Yoon HJ, Suh SW, J Biol Chem. 2006 Jul 7;281(27):18660-7. Epub 2006 May 8. PMID:16682407
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