7p46

Crystal Structure of Xanthomonas campestris Tryptophan 2,3-dioxygenase (TDO)

spinqualitylabelsall models 7p46, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: CYN, GOL, HEM, KYN, TRP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes - tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) - leading initially to the formation of N-formylkynurenine (NFK). In this paper, we present a crystal structure of a bacterial TDO from X. campestris in complex with l-kynurenine, the hydrolysed product of NFK. l-kynurenine is bound at the active site in a similar location to the substrate (l-Trp). Hydrogen bonding interactions with Arg117 and the heme 7-propionate anchor the l-kynurenine molecule into the pocket. A mechanism for the hydrolysis of NFK in the active site is presented. Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase.,Basran J, Booth ES, Campbell LP, Thackray SJ, Jesani MH, Clayden J, Moody PCE, Mowat CG, Kwon H, Raven EL J Inorg Biochem. 2021 Sep 16;225:111604. doi: 10.1016/j.jinorgbio.2021.111604. PMID:34571402 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dioxygenase 3D structures

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