View source for 1yiy


==Aedes aegypti kynurenine aminotransferase==
<StructureSection load='1yiy' size='340' side='right'caption='[[1yiy]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1yiy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIY 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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=1yiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yiy OCA], [https://pdbe.org/1yiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yiy RCSB], [https://www.ebi.ac.uk/pdbsum/1yiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yiy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAT_AEDAE KAT_AEDAE] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) (PubMed:12110301, PubMed:15556614). Also catalyzes the irreversible transamination of several amino acids including cysteine, tyrosine, glutamine, methionine, histidine and phenylalanine (PubMed:15556614). Can use various keto-acids as the amino group acceptor (PubMed:15556614, PubMed:12110301).<ref>PMID:12110301</ref> <ref>PMID:15556614</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/yi/1yiy_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=1yiy ConSurf].
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== Publication Abstract from PubMed ==
Aedes aegypti kynurenine aminotransferase (AeKAT) catalyzes the irreversible transamination of kynurenine to kynurenic acid, the natural antagonist of NMDA and 7-nicotinic acetycholine receptors. Here, we report the crystal structure of AeKAT in its PMP and PLP forms at 1.90 and 1.55 A, respectively. The structure was solved by a combination of single-wavelength anomalous dispersion and molecular replacement approaches. The initial search model in the molecular replacement method was built with the result of single-wavelength anomalous dispersion data from the Br-AeKAT crystal in combination with homology modeling. The solved structure shows that the enzyme is a homodimer, and that the two subunits are stabilized by a number of hydrogen bonds, salts bridges, and hydrophobic interactions. Each subunit is divided into an N-terminal arm and small and large domains. Based on its folding, the enzyme belongs to the prototypical fold type, aminotransferase subgroup I. The three-dimensional structure shows a strictly conserved 'PLP-phosphate binding cup' featuring PLP-dependent enzymes. The interaction between Cys284 (A) and Cys284 (B) is unique in AeKAT, which might explain the cysteine effect of AeKAT activity. Further mutation experiments of this residue are needed to eventually understand the mechanism of the enzyme modulation by cysteine.

Crystal structures of Aedes aegypti kynurenine aminotransferase.,Han Q, Gao YG, Robinson H, Ding H, Wilson S, Li J FEBS J. 2005 May;272(9):2198-206. PMID:15853804<ref>PMID:15853804</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aedes aegypti]]
[[Category: Large Structures]]
[[Category: Ding H]]
[[Category: Gao YG]]
[[Category: Han Q]]
[[Category: Li J]]
[[Category: Robinson H]]
[[Category: Wilson S]]