2nox

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[[Image:2nox.gif|left|200px]]
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{{STRUCTURE_2nox| PDB=2nox | SCENE= }}
{{STRUCTURE_2nox| PDB=2nox | SCENE= }}
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'''Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans'''
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===Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17198384 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17198384}}
==About this Structure==
==About this Structure==
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[[Category: Helical bundle]]
[[Category: Helical bundle]]
[[Category: Heme protein]]
[[Category: Heme protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:43:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:59:52 2008''

Revision as of 01:59, 29 July 2008

Image:2nox.png

Template:STRUCTURE 2nox

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

Template:ABSTRACT PUBMED 17198384

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

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