5k8m

Apo 5-nitroanthranilate aminohydrolase

spinqualitylabelsall models 5k8m, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5k8m is a 4 chain structure with sequence from Bradyrhizobium sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.75Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NAAA_BRASZ Catalyzes the deamination of 5-nitroanthranilate (5NAA) to 5-nitrosalicylate (5NSA), the first step in biodegradation of 5-nitroanthranilate. Publication Abstract from PubMed Nitroaromatic compounds are typically toxic and resistant to degradation. Bradyrhizobium species strain JS329 metabolizes 5-nitroanthranilic acid (5NAA), which is a molecule secreted by Streptomyces scabies, the plant pathogen responsible for potato scab. The first biodegradation enzyme is 5NAA-aminohydrolase (5NAA-A), a metalloprotease family member that converts 5NAA to 5-nitrosalicylic acid. We characterized 5NAA-A biochemically and obtained snapshots of its mechanism. 5NAA-A, an octamer that can use several divalent transition metals for catalysis in vitro, employs a nucleophilic aromatic substitution mechanism. Unexpectedly, the metal in 5NAA-A is labile but is readily loaded in the presence of substrate. 5NAA-A is specific for 5NAA and cannot hydrolyze other tested derivatives, which are likewise poor inhibitors. The 5NAA-A structure and mechanism expand our understanding of the chemical ecology of an agriculturally important plant and pathogen, and will inform bioremediation and biocatalytic approaches to mitigate the environmental and ecological impact of nitroanilines and other challenging substrates. Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution.,Kalyoncu S, Heaner DP Jr, Kurt Z, Bethel CM, Ukachukwu CU, Chakravarthy S, Spain JC, Lieberman RL Nat Chem Biol. 2016 Oct 3. doi: 10.1038/nchembio.2191. PMID:27694799 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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