4cob

Crystal structure kynurenine formamidase from Pseudomonas aeruginosa

spinqualitylabelsall models 4cob, resolution 2.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cob is a 2 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 4co9, 4cog, 4cz1 Activity: Arylformamidase, with EC number 3.5.1.9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KYNB_PSEAE] Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Publication Abstract from PubMed Tryptophan is an important precursor for chemical entities that ultimately support the biosynthesis of key metabolites. The second stage of tryptophan catabolism is catalyzed by kynurenine formamidase, an enzyme that is different between eukaryotes and prokaryotes. Here, we characterize the catalytic properties and present the crystal structures of three bacterial kynurenine formamidases. The structures reveal a new amidase protein fold, a highly organized and distinctive binuclear Zn2+ catalytic centre in a confined, hydrophobic and relatively rigid active site. The structure of a complex with 2-aminoacetophenone delineates aspects of molecular recognition extending to the observation that the substrate itself may be conformationally restricted to assist binding in the confined space of the active site and for subsequent processing. The cations occupy a crowded environment and unlike most Zn2+-dependent enzymes there is little scope to increase coordination number during catalysis. We propose that the presence of a bridging water/hydroxide ligand in conjunction with the placement of an active site histidine supports a distinctive amidation mechanism. Structures of bacterial kynurenine formamidase reveal a crowded binuclear-zinc catalytic site primed to generate a potent nucleophile.,Diaz Saez L, Srikannathasan V, Zoltner M, Hunter WN Biochem J. 2014 Jun 19. PMID:24942958 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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