2nox

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2nox" [edit=sysop:move=sysop])
Current revision (10:17, 30 August 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2nox.png|left|200px]]
 
-
{{STRUCTURE_2nox| PDB=2nox | SCENE= }}
+
==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 [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='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>
 +
<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'>[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>
 +
== Function ==
 +
[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 ==
 +
[[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].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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 of tryptophan 2,3-dioxygenase from Ralstonia metallidurans===
+
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>
-
{{ABSTRACT_PUBMED_17198384}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2nox" style="background-color:#fffaf0;"></div>
-
==About this Structure==
+
==See Also==
-
[[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].
+
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:017198384</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Cupriavidus metallidurans]]
[[Category: Cupriavidus metallidurans]]
-
[[Category: Tryptophan 2,3-dioxygenase]]
+
[[Category: Large Structures]]
-
[[Category: Bale, S.]]
+
[[Category: Bale S]]
-
[[Category: Begley, T P.]]
+
[[Category: Begley TP]]
-
[[Category: Crane, B R.]]
+
[[Category: Crane BR]]
-
[[Category: Ealick, S E.]]
+
[[Category: Ealick SE]]
-
[[Category: Kang, S A.]]
+
[[Category: Kang SA]]
-
[[Category: Mukherjee, T.]]
+
[[Category: Mukherjee T]]
-
[[Category: Zhang, Y.]]
+
[[Category: Zhang Y]]
-
[[Category: Helical bundle]]
+
-
[[Category: Heme protein]]
+
-
[[Category: Oxidoreductase]]
+

Current revision

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

PDB ID 2nox

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nox"
Personal tools