2nox

Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metalliduransCrystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans

Structural highlights

2nox is a 16 chain structure with sequence from Atcc 43123. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Tryptophan 2,3-dioxygenase, with EC number 1.13.11.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[T23O_RALME] Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring.[HAMAP-Rule:MF_01972]^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kurnasov O, Goral V, Colabroy K, Gerdes S, Anantha S, Osterman A, Begley TP. NAD biosynthesis: identification of the tryptophan to quinolinate pathway in bacteria. Chem Biol. 2003 Dec;10(12):1195-204. PMID:14700627
↑ Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095
↑ Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095

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OCA

[1] Kurnasov O, Goral V, Colabroy K, Gerdes S, Anantha S, Osterman A, Begley TP. NAD biosynthesis: identification of the tryptophan to quinolinate pathway in bacteria. Chem Biol. 2003 Dec;10(12):1195-204. PMID:14700627

[2] Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095

[3] Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095

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