2nox

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(New page: 200px<br /><applet load="2nox" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nox, resolution 2.400&Aring;" /> '''Crystal structure o...)
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[[Image:2nox.gif|left|200px]]<br /><applet load="2nox" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2nox, resolution 2.400&Aring;" />
 
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'''Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans'''<br />
 
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==Overview==
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==Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans==
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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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<StructureSection load='2nox' size='340' side='right'caption='[[2nox]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2nox]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans Cupriavidus metallidurans]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2NOX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nox OCA], [https://pdbe.org/2nox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nox RCSB], [https://www.ebi.ac.uk/pdbsum/2nox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nox ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/T23O_CUPMC T23O_CUPMC] Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.[HAMAP-Rule:MF_01972]<ref>PMID:17198384</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/2nox_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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>
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2NOX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans Cupriavidus metallidurans] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17198384 17198384]
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</div>
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[[Category: Cupriavidus metallidurans]]
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<div class="pdbe-citations 2nox" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Tryptophan 2,3-dioxygenase]]
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[[Category: Bale, S.]]
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[[Category: Begley, T.P.]]
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[[Category: Crane, B.R.]]
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[[Category: Ealick, S.E.]]
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[[Category: Kang, S.A.]]
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[[Category: Mukherjee, T.]]
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[[Category: Zhang, Y.]]
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[[Category: HEM]]
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[[Category: helical bundle]]
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[[Category: heme protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:57:02 2008''
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==See Also==
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cupriavidus metallidurans]]
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[[Category: Large Structures]]
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[[Category: Bale S]]
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[[Category: Begley TP]]
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[[Category: Crane BR]]
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[[Category: Ealick SE]]
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[[Category: Kang SA]]
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[[Category: Mukherjee T]]
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[[Category: Zhang Y]]

Current revision

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

PDB ID 2nox

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