2nox: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nox]] is a 16 chain structure with sequence from [http://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 [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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NOX FirstGlance]. <br> | ||
</td></tr><tr><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='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><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='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><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://www.rcsb.org/pdb/explore.do?structureId=2nox RCSB], [http://www.ebi.ac.uk/pdbsum/2nox PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=2nox RCSB], [http://www.ebi.ac.uk/pdbsum/2nox PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Cupriavidus metallidurans]] | [[Category: Cupriavidus metallidurans]] | ||
[[Category: Tryptophan 2,3-dioxygenase]] | [[Category: Tryptophan 2,3-dioxygenase]] | ||
[[Category: Bale, S | [[Category: Bale, S]] | ||
[[Category: Begley, T P | [[Category: Begley, T P]] | ||
[[Category: Crane, B R | [[Category: Crane, B R]] | ||
[[Category: Ealick, S E | [[Category: Ealick, S E]] | ||
[[Category: Kang, S A | [[Category: Kang, S A]] | ||
[[Category: Mukherjee, T | [[Category: Mukherjee, T]] | ||
[[Category: Zhang, Y | [[Category: Zhang, Y]] | ||
[[Category: Helical bundle]] | [[Category: Helical bundle]] | ||
[[Category: Heme protein]] | [[Category: Heme protein]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 18:42, 19 January 2015
Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metalliduransCrystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans
Structural highlights
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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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