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1arg

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[[Image:1arg.gif|left|200px]]<br /><applet load="1arg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1arg, resolution 2.2&Aring;" />
 
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'''ASPARTATE AMINOTRANSFERASE, PHOSPHO-5'-PYRIDOXYL ASPARTATE COMPLEX'''<br />
 
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==Overview==
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==Aspartate aminotransferase, phospho-5'-pyridoxyl aspartate complex==
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The electron distribution in the coenzyme-substrate adduct of aspartate aminotransferase was changed by replacing active-site Arg386 with alanine and introducing a new arginine residue nearby. [Y225R, R386A]Aspartate aminotransferase decarboxylates L-aspartate to L-alanine (kcat = 0.04 s-1), while its transaminase activity towards dicarboxylic amino acids is decreased by three orders of magnitude (kcat = 0.19 s-1). Molecular-dynamics simulations based on the crystal structure of the mutant enzyme suggest that a new hydrogen bond to the imine N atom of the pyridoxal-5'-phosphate- aspartate adduct and an altered electrostatic potential around its beta-carboxylate group underlie the 650,000-fold increase in the ratio of beta-decarboxylase/transaminase activity.
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<StructureSection load='1arg' size='340' side='right'caption='[[1arg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1arg]] 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=1ARG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ARG 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]] 2.2&#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=PPD:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC+ACID'>PPD</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=1arg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1arg OCA], [https://pdbe.org/1arg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1arg RCSB], [https://www.ebi.ac.uk/pdbsum/1arg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1arg 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/ar/1arg_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=1arg ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ARG 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 <scene name='pdbligand=PPD:'>PPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1ARG OCA].
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme., Graber R, Kasper P, Malashkevich VN, Sandmeier E, Berger P, Gehring H, Jansonius JN, Christen P, Eur J Biochem. 1995 Sep 1;232(2):686-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7556224 7556224]
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[[Category: Aspartate transaminase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Jansonius, J N.]]
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[[Category: Jansonius JN]]
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[[Category: Malashkevich, V N.]]
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[[Category: Malashkevich VN]]
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[[Category: PPD]]
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[[Category: transferase (aminotransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:35 2008''
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Current revision

Aspartate aminotransferase, phospho-5'-pyridoxyl aspartate complex

PDB ID 1arg

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