2nox: Difference between revisions
New page: left|200px<br /><applet load="2nox" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nox, resolution 2.400Å" /> '''Crystal structure o... |
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==Overview== | ==Overview== | ||
The structure of tryptophan 2,3-dioxygenase (TDO) from Ralstonia | 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== | ==About this Structure== | ||
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[[Category: Tryptophan 2,3-dioxygenase]] | [[Category: Tryptophan 2,3-dioxygenase]] | ||
[[Category: Bale, S.]] | [[Category: Bale, S.]] | ||
[[Category: Begley, T | [[Category: Begley, T P.]] | ||
[[Category: Crane, B | [[Category: Crane, B R.]] | ||
[[Category: Ealick, S | [[Category: Ealick, S E.]] | ||
[[Category: Kang, S | [[Category: Kang, S A.]] | ||
[[Category: Mukherjee, T.]] | [[Category: Mukherjee, T.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
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[[Category: heme protein]] | [[Category: heme protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:16 2008'' | ||
Revision as of 16:09, 21 February 2008
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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 with HEM as ligand. Active as Tryptophan 2,3-dioxygenase, with EC number 1.13.11.11 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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