2nox: Difference between revisions

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[[Image:2nox.~~gif~~|left|200px]]

[[Image:2nox.png|left|200px]]

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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==~~

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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.

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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==About this Structure==

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[[Category: Helical bundle]]

[[Category: Heme protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 09~~:43:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:59:52 2008''

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-[[Image:2nox.gif|left|200px]]
+{{Seed}}
+[[Image:2nox.png|left|200px]]
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 {{STRUCTURE_2nox|  PDB=2nox  |  SCENE=  }}
-'''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.
+-->
+{{ABSTRACT_PUBMED_17198384}}
 ==About this Structure==
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 [[Category: Helical bundle]]
 [[Category: Heme protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:43:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:59:52 2008''