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| | <StructureSection load='2nox' size='340' side='right'caption='[[2nox]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2nox' size='340' side='right'caption='[[2nox]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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='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> |
| - | <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> | + | <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> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43123]] | + | [[Category: Cupriavidus metallidurans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tryptophan 2,3-dioxygenase]]
| + | [[Category: Bale S]] |
| - | [[Category: Bale, S]] | + | [[Category: Begley TP]] |
| - | [[Category: Begley, T P]] | + | [[Category: Crane BR]] |
| - | [[Category: Crane, B R]] | + | [[Category: Ealick SE]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Kang SA]] |
| - | [[Category: Kang, S A]] | + | [[Category: Mukherjee T]] |
| - | [[Category: Mukherjee, T]] | + | [[Category: Zhang Y]] |
| - | [[Category: Zhang, Y]] | + | |
| - | [[Category: Helical bundle]]
| + | |
| - | [[Category: Heme protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
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][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095
- ↑ Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE. Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384 doi:10.1021/bi0620095
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