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1aaw

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[[Image:1aaw.jpg|left|200px]]
 
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==THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI==
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The line below this paragraph, containing "STRUCTURE_1aaw", creates the "Structure Box" on the page.
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<StructureSection load='1aaw' size='340' side='right'caption='[[1aaw]], [[Resolution|resolution]] 2.40&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'>[[1aaw]] is a 1 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=1AAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AAW 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]] 2.4&#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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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{{STRUCTURE_1aaw| PDB=1aaw | 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=1aaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aaw OCA], [https://pdbe.org/1aaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aaw RCSB], [https://www.ebi.ac.uk/pdbsum/1aaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aaw 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/aa/1aaw_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=1aaw ConSurf].
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<div style="clear:both"></div>
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'''THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI'''
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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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Two refined crystal structures of aspartate aminotransferase from E. coli are reported. The wild type enzyme is in the pyridoxal phosphate (PLP) form and its structure has been determined to 2.4 A resolution, refined to an R-factor of 23.2%. The structure of the Arg292Asp mutant has been determined at 2.8 A resolution, refined to an R-factor of 20.3%. The wild type and mutant crystals are isomorphous and the two structures are very similar, with only minor changes in positions of important active site residues. As residue Arg292 is primarily responsible for the substrate charge specificity in the wild type enzyme, the mutant containing a charge reversal at this position might be expected to catalyze transamination of arginine as efficiently as the wild type enzyme effects transamination of aspartate [Cronin, C.N. and Kirsch, J.F. (1988) Biochemistry, 27, 4572-4579]. This mutant does in fact prefer arginine over aspartate as a substrate, however, the rate of catalysis is much slower than that of the wild type enzyme with its physiological substrate, aspartate. A comparison of these two structures indicates that the poorer catalytic efficiency of R292D, when presented with arginine, is not due to a gross conformational difference, but is rather a consequence of both small side chain and main chain reorientations and the pre-existing active site polar environment, which greatly favors the wild type ion pair interaction.
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==About this Structure==
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1AAW 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=1AAW OCA].
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==Reference==
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The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli., Almo SC, Smith DL, Danishefsky AT, Ringe D, Protein Eng. 1994 Mar;7(3):405-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7909946 7909946]
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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: Almo, S C.]]
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[[Category: Almo SC]]
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[[Category: Danishefsky, A T.]]
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[[Category: Danishefsky AT]]
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[[Category: Ringe, D.]]
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[[Category: Ringe D]]
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[[Category: Smith, D L.]]
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[[Category: Smith DL]]
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[[Category: Aminotransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:03:21 2008''
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Current revision

THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI

PDB ID 1aaw

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