View source for 7p46


==Crystal Structure of Xanthomonas campestris Tryptophan 2,3-dioxygenase (TDO)==
<StructureSection load='7p46' size='340' side='right'caption='[[7p46]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P46 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=KYN:(2S)-2-AMINO-4-(2-AMINOPHENYL)-4-OXOBUTANOIC+ACID'>KYN</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></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=7p46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p46 OCA], [https://pdbe.org/7p46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p46 RCSB], [https://www.ebi.ac.uk/pdbsum/7p46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p46 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes - tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) - leading initially to the formation of N-formylkynurenine (NFK). In this paper, we present a crystal structure of a bacterial TDO from X. campestris in complex with l-kynurenine, the hydrolysed product of NFK. l-kynurenine is bound at the active site in a similar location to the substrate (l-Trp). Hydrogen bonding interactions with Arg117 and the heme 7-propionate anchor the l-kynurenine molecule into the pocket. A mechanism for the hydrolysis of NFK in the active site is presented.

Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase.,Basran J, Booth ES, Campbell LP, Thackray SJ, Jesani MH, Clayden J, Moody PCE, Mowat CG, Kwon H, Raven EL J Inorg Biochem. 2021 Sep 16;225:111604. doi: 10.1016/j.jinorgbio.2021.111604. PMID:34571402<ref>PMID:34571402</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7p46" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Basran J]]
[[Category: Booth ES]]
[[Category: Campbell LP]]
[[Category: Kwon H]]
[[Category: Moody PCE]]
[[Category: Mowat CG]]
[[Category: Raven EL]]
[[Category: Thackray SJ]]