2ch1

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[[Image:2ch1.png|left|200px]]
 
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{{STRUCTURE_2ch1| PDB=2ch1 | SCENE= }}
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==Structure of Anopheles gambiae 3-hydroxykynurenine transaminase==
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<StructureSection load='2ch1' size='340' side='right'caption='[[2ch1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2ch1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CH1 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=2ch1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ch1 OCA], [https://pdbe.org/2ch1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ch1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ch1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ch1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HKT_ANOGA HKT_ANOGA] Catalyzes the pyridoxal 5'-phosphate-dependent transamination of both 3-hydroxykynurenine and L-kynurenine to xanthurenic acid and kynurenic acid, respectively, preferentially using the alpha-ketoacid glyoxylate as the amino group acceptor (PubMed:16262702). Although glyoxylate is the preferred amino group acceptor, transamination of 3-hydroxykynurenine also works with pyruvate as the amino acceptor in vitro (PubMed:16262702). Involved in the detoxification of cytotoxic metabolite 3-hydroxykynurenine generated by the hydroxylation of L-kynurenine, an intermediate in the tryptophan catabolism pathway (PubMed:16262702). The Plasmodium parasite uses xanthurenic acid produced in the midgut to activate its gametocytes ingested during a blood meal (Probable). Also catalyzes, although with a lesser efficiency, the transamination of alanine with glyoxylate as an amino group acceptor (By similarity). May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the diet (By similarity).[UniProtKB:Q0IG34]<ref>PMID:16262702</ref> <ref>PMID:16262702</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/ch/2ch1_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=2ch1 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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In Anopheles gambiae, the vector for the most deadly malaria parasite Plasmodium falciparum, xanthurenic acid (XA) plays a key role in parasite gametogenesis and fertility. In mosquitoes, XA is produced by transamination of 3-hydroxykynurenine (3-HK), a reaction that represents the main route to prevent the accumulation of the potentially toxic 3-HK excess. Interfering with XA metabolism in A. gambiae therefore appears an attractive avenue for the development of malaria transmission-blocking drugs and insecticides. We have determined the crystal structure of A. gambiae 3-HK transaminase in its pyridoxal 5'-phosphate form and in complex with a newly synthesized competitive enzyme inhibitor. Structural inspection of the enzyme active site reveals the key molecular determinants for ligand recognition and catalysis. Major contributions toward inhibitor binding are provided by a salt bridge between the inhibitor carboxylate and Arg-356 and by a remarkable hydrogen bond network involving the anthranilic moiety of the inhibitor and backbone atoms of residues Gly-25 and Asn-44. This study may be useful for the structure-based design of specific enzyme inhibitors of potential interest as antimalarial agents.
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===STRUCTURE OF ANOPHELES GAMBIAE 3-HYDROXYKYNURENINE TRANSAMINASE===
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Crystal structure of the Anopheles gambiae 3-hydroxykynurenine transaminase.,Rossi F, Garavaglia S, Giovenzana GB, Arca B, Li J, Rizzi M Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5711-6. Epub 2006 Apr 3. PMID:16585514<ref>PMID:16585514</ref>
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{{ABSTRACT_PUBMED_16585514}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2ch1" style="background-color:#fffaf0;"></div>
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[[2ch1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CH1 OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016585514</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Anopheles gambiae]]
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[[Category: Arca, B.]]
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[[Category: Garavaglia, S.]]
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[[Category: Giovenzana, G B.]]
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[[Category: Li, J.]]
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[[Category: Rizzi, M.]]
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[[Category: Rossi, F.]]
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[[Category: 3-hydroxykynurenine transaminase]]
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[[Category: Anopheles gambiae]]
[[Category: Anopheles gambiae]]
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[[Category: Kynurenine pathway]]
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[[Category: Large Structures]]
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[[Category: Plp-enzyme]]
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[[Category: Arca B]]
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[[Category: Transferase]]
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[[Category: Garavaglia S]]
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[[Category: Giovenzana GB]]
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[[Category: Li J]]
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[[Category: Rizzi M]]
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[[Category: Rossi F]]

Current revision

Structure of Anopheles gambiae 3-hydroxykynurenine transaminase

PDB ID 2ch1

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