2nox: Difference between revisions

Revision as of 04:59, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nox.png

Template:STRUCTURE 2nox

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

Template:ABSTRACT PUBMED 17198384

About this StructureAbout this Structure

2NOX is a Single protein structure of sequence from Cupriavidus metallidurans. 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 Jul 29 04:59:52 2008

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OCA

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-'''Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17198384}}, adds the Publication Abstract to the page
+(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==
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 [[Category: Helical bundle]]
 [[Category: Heme protein]]
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