2nox
|
Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans
OverviewOverview
The structure of tryptophan 2,3-dioxygenase (TDO) from Ralstonia, metallidurans was determined at 2.4 A. TDO catalyzes the irreversible, oxidation of l-tryptophan to N-formyl kynurenine, which is the initial, step in tryptophan catabolism. TDO is a heme-containing enzyme and is, highly specific for its substrate l-tryptophan. The structure is a, tetramer with a heme cofactor bound at each active site. The monomeric, fold, as well as the heme binding site, is similar to that of the large, domain of indoleamine 2,3-dioxygenase, an enzyme that catalyzes the same, reaction except with a broader substrate tolerance. Modeling of the, putative (S)-tryptophan hydroperoxide intermediate into the active site, as well as substrate analogue and mutagenesis studies, are consistent with, a Criegee mechanism for the reaction.
About this StructureAbout this Structure
2NOX is a Single protein structure of sequence from Cupriavidus metallidurans with as ligand. Active as Tryptophan 2,3-dioxygenase, with EC number 1.13.11.11 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis., Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE, Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384
Page seeded by OCA on Tue Jan 29 20:57:02 2008