3gl2 | pdb_00003gl2

Crystal structure of dicamba monooxygenase bound to dicamba

spinqualitylabelsall models 3gl2, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gl2 is a 3 chain structure with sequence from "pseudomonas_maltophilia"_hugh_and_ryschenkow_1961 "pseudomonas maltophilia" hugh and ryschenkow 1961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: D3M, FE, FES Related: 3gke, 3gl0 Gene: ddmC ("Pseudomonas maltophilia" Hugh and Ryschenkow 1961) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Dicamba (3,6-dichloro-2-methoxybenzoic acid) is a widely used herbicide that is efficiently degraded by soil microbes. These microbes use a novel Rieske nonheme oxygenase, dicamba monooxygenase (DMO), to catalyze the oxidative demethylation of dicamba to 3,6-dichlorosalicylic acid (DCSA) and formaldehyde. We have determined the crystal structures of DMO in the free state, bound to its substrate dicamba, and bound to the product DCSA at 2.10-1.75 A resolution. The structures show that the DMO active site uses a combination of extensive hydrogen bonding and steric interactions to correctly orient chlorinated, ortho-substituted benzoic-acid-like substrates for catalysis. Unlike other Rieske aromatic oxygenases, DMO oxygenates the exocyclic methyl group, rather than the aromatic ring, of its substrate. This first crystal structure of a Rieske demethylase shows that the Rieske oxygenase structural scaffold can be co-opted to perform varied types of reactions on xenobiotic substrates. Crystal structure of dicamba monooxygenase: a Rieske nonheme oxygenase that catalyzes oxidative demethylation.,Dumitru R, Jiang WZ, Weeks DP, Wilson MA J Mol Biol. 2009 Sep 18;392(2):498-510. Epub 2009 Jul 15. PMID:19616011 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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