2nox
From Proteopedia
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'''Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans''' | '''Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans''' | ||
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[[Category: Mukherjee, T.]] | [[Category: Mukherjee, T.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
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| - | [[Category: | + | [[Category: Heme protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:43:26 2008'' | |
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Revision as of 06:43, 4 May 2008
Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans
Overview
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 Structure
2NOX is a Single protein structure of sequence from Cupriavidus metallidurans. Full crystallographic information is available from OCA.
Reference
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 Sun May 4 09:43:26 2008
