View source for 2nox


==Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans==
<StructureSection load='2nox' size='340' side='right' caption='[[2nox]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2nox]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43123 Atcc 43123]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NOX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_2,3-dioxygenase Tryptophan 2,3-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.11 1.13.11.11] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nox OCA], [http://pdbe.org/2nox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nox RCSB], [http://www.ebi.ac.uk/pdbsum/2nox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nox ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/T23O_RALME T23O_RALME]] Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring.[HAMAP-Rule:MF_01972]<ref>PMID:14700627</ref> <ref>PMID:17198384</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/2nox_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nox ConSurf].
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:17198384</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2nox" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 43123]]
[[Category: Tryptophan 2,3-dioxygenase]]
[[Category: Bale, S]]
[[Category: Begley, T P]]
[[Category: Crane, B R]]
[[Category: Ealick, S E]]
[[Category: Kang, S A]]
[[Category: Mukherjee, T]]
[[Category: Zhang, Y]]
[[Category: Helical bundle]]
[[Category: Heme protein]]
[[Category: Oxidoreductase]]