1yiz

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(New page: 200px<br /><applet load="1yiz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yiz, resolution 1.55&Aring;" /> '''Aedes aegypti kynure...)
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[[Image:1yiz.gif|left|200px]]<br /><applet load="1yiz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yiz, resolution 1.55&Aring;" />
 
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'''Aedes aegypti kynurenine aminotrasferase'''<br />
 
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==Overview==
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==Aedes aegypti kynurenine aminotrasferase==
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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.
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<StructureSection load='1yiz' size='340' side='right'caption='[[1yiz]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1yiz]] 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=1YIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIZ FirstGlance]. <br>
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1YIZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti] with BR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YIZ OCA].
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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]] 1.55&#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=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
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==Reference==
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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=1yiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yiz OCA], [https://pdbe.org/1yiz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yiz RCSB], [https://www.ebi.ac.uk/pdbsum/1yiz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yiz ProSAT]</span></td></tr>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15853804 15853804]
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</table>
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== Function ==
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[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>
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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/yi/1yiz_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=1yiz ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Aedes aegypti]]
[[Category: Aedes aegypti]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ding, H.]]
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[[Category: Ding H]]
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[[Category: Gao, Y.G.]]
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[[Category: Gao YG]]
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[[Category: Han, Q.]]
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[[Category: Han Q]]
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[[Category: Li, J.]]
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[[Category: Li J]]
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[[Category: Robinson, H.]]
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[[Category: Robinson H]]
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[[Category: Wilson, S.]]
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[[Category: Wilson S]]
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[[Category: BR]]
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[[Category: aedes]]
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[[Category: kynurenic acid]]
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[[Category: kynurenine]]
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[[Category: kynurenine aminotransferase]]
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[[Category: mosquito]]
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[[Category: plp]]
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[[Category: plp-enzyme]]
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[[Category: pyridoxal phosphate]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:11:07 2007''
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Current revision

Aedes aegypti kynurenine aminotrasferase

PDB ID 1yiz

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