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3dc1

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{{Seed}}
 
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[[Image:3dc1.png|left|200px]]
 
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==Crystal structure of kynurenine aminotransferase II complex with alpha-ketoglutarate==
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The line below this paragraph, containing "STRUCTURE_3dc1", creates the "Structure Box" on the page.
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<StructureSection load='3dc1' size='340' side='right'caption='[[3dc1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3dc1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DC1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.5&#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=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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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{{STRUCTURE_3dc1| PDB=3dc1 | SCENE= }}
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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=3dc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dc1 OCA], [https://pdbe.org/3dc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dc1 RCSB], [https://www.ebi.ac.uk/pdbsum/3dc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dc1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AADAT_HUMAN AADAT_HUMAN] Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).<ref>PMID:18620547</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/dc/3dc1_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=3dc1 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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KAT (kynurenine aminotransferase) II is a primary enzyme in the brain for catalysing the transamination of kynurenine to KYNA (kynurenic acid). KYNA is the only known endogenous antagonist of the N-methyl-D-aspartate receptor. The enzyme also catalyses the transamination of aminoadipate to alpha-oxoadipate; therefore it was initially named AADAT (aminoadipate aminotransferase). As an endotoxin, aminoadipate influences various elements of glutamatergic neurotransmission and kills primary astrocytes in the brain. A number of studies dealing with the biochemical and functional characteristics of this enzyme exist in the literature, but a systematic assessment of KAT II addressing its substrate profile and kinetic properties has not been performed. The present study examines the biochemical and structural characterization of a human KAT II/AADAT. Substrate screening of human KAT II revealed that the enzyme has a very broad substrate specificity, is capable of catalysing the transamination of 16 out of 24 tested amino acids and could utilize all 16 tested alpha-oxo acids as amino-group acceptors. Kinetic analysis of human KAT II demonstrated its catalytic efficiency for individual amino-group donors and acceptors, providing information as to its preferred substrate affinity. Structural analysis of the human KAT II complex with alpha-oxoglutaric acid revealed a conformational change of an N-terminal fraction, residues 15-33, that is able to adapt to different substrate sizes, which provides a structural basis for its broad substrate specificity.
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===Crystal structure of kynurenine aminotransferase II complex with alpha-ketoglutarate===
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Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II.,Han Q, Cai T, Tagle DA, Robinson H, Li J Biosci Rep. 2008 Aug;28(4):205-15. PMID:18620547<ref>PMID:18620547</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_18620547}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3dc1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18620547 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18620547}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3DC1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DC1 OCA].
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==Reference==
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Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II., Han Q, Cai T, Tagle DA, Robinson H, Li J, Biosci Rep. 2008 Aug;28(4):205-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18620547 18620547]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cai, T.]]
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[[Category: Cai T]]
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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: Tagle, D A.]]
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[[Category: Tagle DA]]
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[[Category: Alpha & beta protein]]
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[[Category: Alternative splicing]]
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[[Category: Aminotransferase]]
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[[Category: Mitochondrion]]
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[[Category: Multifunctional enzyme]]
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[[Category: Plp-dependent transferase]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Transferase]]
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[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 10 09:11:31 2008''
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Current revision

Crystal structure of kynurenine aminotransferase II complex with alpha-ketoglutarate

PDB ID 3dc1

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