7P46
Crystal Structure of Xanthomonas campestris Tryptophan 2,3-dioxygenase (TDO)
Summary for 7P46
| Entry DOI | 10.2210/pdb7p46/pdb |
| Descriptor | Tryptophan 2,3-dioxygenase, PROTOPORPHYRIN IX CONTAINING FE, CYANIDE ION, ... (7 entities in total) |
| Functional Keywords | dioxygenase, cyanide, kynurenine, oxidoreductase |
| Biological source | Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) |
| Total number of polymer chains | 8 |
| Total formula weight | 273215.48 |
| Authors | Kwon, H.,Basran, J.,Booth, E.S.,Campbell, L.P.,Thackray, S.J.,Moody, P.C.E.,Mowat, C.G.,Raven, E.L. (deposition date: 2021-07-09, release date: 2021-10-06, Last modification date: 2024-01-31) |
| Primary citation | Basran, J.,Booth, E.S.,Campbell, L.P.,Thackray, S.J.,Jesani, M.H.,Clayden, J.,Moody, P.C.E.,Mowat, C.G.,Kwon, H.,Raven, E.L. Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase. J.Inorg.Biochem., 225:111604-111604, 2021 Cited by PubMed Abstract: 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. PubMed: 34571402DOI: 10.1016/j.jinorgbio.2021.111604 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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