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1ahg

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[[Image:1ahg.gif|left|200px]]
 
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{{Structure
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==ASPARTATE AMINOTRANSFERASE HEXAMUTANT==
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|PDB= 1ahg |SIZE=350|CAPTION= <scene name='initialview01'>1ahg</scene>, resolution 2.5&Aring;
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<StructureSection load='1ahg' size='340' side='right'caption='[[1ahg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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<table><tr><td colspan='2'>[[1ahg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHG FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=TYR:TYROSINE'>TYR</scene></td></tr>
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|DOMAIN=
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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=1ahg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahg OCA], [https://pdbe.org/1ahg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahg RCSB], [https://www.ebi.ac.uk/pdbsum/1ahg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahg ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ahg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahg OCA], [http://www.ebi.ac.uk/pdbsum/1ahg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ahg RCSB]</span>
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== Function ==
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}}
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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/1ahg_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=1ahg ConSurf].
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<div style="clear:both"></div>
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'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''
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==See Also==
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Jansonius JN]]
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1AHG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHG OCA].
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[[Category: Malashkevich VN]]
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/7664122 7664122]
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[[Category: Aspartate transaminase]]
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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: transferase (aminotransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:40:16 2008''
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Current revision

ASPARTATE AMINOTRANSFERASE HEXAMUTANT

PDB ID 1ahg

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