1ahy

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(New page: 200px<br /><applet load="1ahy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ahy, resolution 2.3&Aring;" /> '''ASPARTATE AMINOTRANSF...)
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[[Image:1ahy.gif|left|200px]]<br /><applet load="1ahy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ahy, resolution 2.3&Aring;" />
 
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'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''<br />
 
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==Overview==
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==ASPARTATE AMINOTRANSFERASE HEXAMUTANT==
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Mutation of six residues of Escherichia coli aspartate aminotransferase, results in substantial acquisition of the transamination properties of, tyrosine amino-transferase without loss of aspartate transaminase, activity. X-ray crystallographic analysis of key inhibitor complexes of, the hexamutant reveals the structural basis for this substrate, selectivity. It appears that tyrosine aminotransferase achieves nearly, equal affinities for a wide range of amino acids by an unusual, conformational switch. An active-site arginine residue either shifts its, position to electrostatically interact with charged substrates or moves, aside to allow access of aromatic ligands.
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<StructureSection load='1ahy' size='340' side='right'caption='[[1ahy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ahy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHY 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]] 2.3&#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=MAE:MALEIC+ACID'>MAE</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=1ahy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahy OCA], [https://pdbe.org/1ahy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahy RCSB], [https://www.ebi.ac.uk/pdbsum/1ahy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
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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/ah/1ahy_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=1ahy 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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Mutation of six residues of Escherichia coli aspartate aminotransferase results in substantial acquisition of the transamination properties of tyrosine amino-transferase without loss of aspartate transaminase activity. X-ray crystallographic analysis of key inhibitor complexes of the hexamutant reveals the structural basis for this substrate selectivity. It appears that tyrosine aminotransferase achieves nearly equal affinities for a wide range of amino acids by an unusual conformational switch. An active-site arginine residue either shifts its position to electrostatically interact with charged substrates or moves aside to allow access of aromatic ligands.
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==About this Structure==
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Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.,Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN Nat Struct Biol. 1995 Jul;2(7):548-53. PMID:7664122<ref>PMID:7664122</ref>
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1AHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PLP and MAE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AHY OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase., Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN, Nat Struct Biol. 1995 Jul;2(7):548-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7664122 7664122]
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</div>
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[[Category: Aspartate transaminase]]
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<div class="pdbe-citations 1ahy" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Jansonius, J.N.]]
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[[Category: Malashkevich, V.N.]]
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[[Category: MAE]]
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[[Category: PLP]]
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[[Category: transferase (aminotransferase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:52:17 2007''
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==See Also==
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Jansonius JN]]
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[[Category: Malashkevich VN]]

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ASPARTATE AMINOTRANSFERASE HEXAMUTANT

PDB ID 1ahy

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