5HEI
Structure of B. megaterium NfrA2
Summary for 5HEI
| Entry DOI | 10.2210/pdb5hei/pdb |
| Descriptor | NfrA2, FLAVIN MONONUCLEOTIDE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total) |
| Functional Keywords | nitroreductase enzyme, dimer, oxidoreductase |
| Biological source | Bacillus megaterium |
| Total number of polymer chains | 8 |
| Total formula weight | 229140.43 |
| Authors | Vigouroux, A.,Morera, S. (deposition date: 2016-01-06, release date: 2016-04-06, Last modification date: 2024-01-10) |
| Primary citation | Carles, L.,Besse-Hoggan, P.,Joly, M.,Vigouroux, A.,Morera, S.,Batisson, I. Functional and structural characterization of two Bacillus megaterium nitroreductases biotransforming the herbicide mesotrione. Biochem.J., 473:1443-1453, 2016 Cited by PubMed Abstract: Mesotrione is a selective herbicide belonging to the triketone family, commonly used on maize cultures since 2003. A mesotrione-transforming Bacillus megaterium Mes11 strain isolated from an agricultural soil was used as a model to identify the key enzymes initiating the biotransformation of this herbicide. Two enzymes (called NfrA1 and NfrA2/YcnD) were identified, and functionally and structurally characterized. Both belong to the NfsA FRP family of the nitro-FMN reductase superfamily (type I oxygen-insensitive nitroreductase) and show optimal pH and temperature of 6-6.5 and 23-25°C, respectively. Both undergo a Ping Pong Bi Bi mechanism, with NADPH and NADPH/NADH as cofactors for NfrA1 and NfrA2/YcnD, respectively. It is interesting that both can also reduce various nitro compounds including pesticides, antibiotics, one prodrug and 4-methylsulfonyl-2-nitrobenzoic acid, one of the mesotrione metabolites retrieved from the environment. The present study constitutes the first identification of mesotrione-transforming enzymes. These enzymes (or their corresponding genes) could be used as biomarkers to predict the capacity of ecosystems to transform mesotrione and assess their contamination by both the parent molecule and/or the metabolites. PubMed: 27005432DOI: 10.1042/BJ20151366 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.84 Å) |
Structure validation
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