2GJN
crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate
Summary for 2GJN
| Entry DOI | 10.2210/pdb2gjn/pdb |
| Descriptor | hypothetical protein PA1024, FLAVIN MONONUCLEOTIDE, 2-NITROPROPANE, ... (4 entities in total) |
| Functional Keywords | 2-nitropropane dioxygenase, fmn, 2-nitropropane, substrate, oxidoreductase |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 1 |
| Total formula weight | 35406.34 |
| Authors | Suh, S.W. (deposition date: 2006-03-31, release date: 2006-05-16, Last modification date: 2024-03-13) |
| Primary citation | Ha, J.Y.,Min, J.Y.,Lee, S.K.,Kim, H.S.,Kim, J.,Kim, K.H.,Lee, H.H.,Kim, H.K.,Yoon, H.J.,Suh, S.W. Crystal Structure of 2-Nitropropane Dioxygenase Complexed with FMN and Substrate: identification of the catalytic base J.Biol.Chem., 281:18660-18667, 2006 Cited by PubMed Abstract: 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. PubMed: 16682407DOI: 10.1074/jbc.M601658200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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