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New page: left|200px<br /><applet load="3aat" size="450" color="white" frame="true" align="right" spinBox="true" caption="3aat, resolution 2.8Å" /> '''ACTIVITY AND STRUCTUR...
 
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[[Image:3aat.gif|left|200px]]<br /><applet load="3aat" size="450" color="white" frame="true" align="right" spinBox="true"
caption="3aat, resolution 2.8&Aring;" />
'''ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE'''<br />


==Overview==
==ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE==
Arginine-386, the active-site residue of Escherichia coli aspartate, aminotransferase (EC 2.6.1.1) that binds the substrate alpha-carboxylate, was replaced with tyrosine and phenylalanine by site-directed mutagenesis., This experiment was undertaken to elucidate the roles of particular, enzyme-substrate interactions in triggering the substrate-induced, conformational change in the enzyme. The activity and crystal structure of, the resulting mutants were examined. The apparent second-order rate, constants of both of these mutants are reduced by more than 5 orders of, magnitude as compared to that of wild-type enzyme, though R386Y is, slightly more active than R386F. The 2.5-A resolution structure of R386F, in its native state was determined by using difference Fourier methods., The overall structure is very similar to that of the wild-type enzyme in, the open conformation. The position of the Phe-386 side chain, however, appears to shift with respect to that of Arg-386 in the wild-type enzyme, and to form new contacts with neighboring residues.
<StructureSection load='3aat' size='340' side='right'caption='[[3aat]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3aat]] 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=3AAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<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=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aat OCA], [https://pdbe.org/3aat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aat RCSB], [https://www.ebi.ac.uk/pdbsum/3aat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aat ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/3aat_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3aat ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arginine-386, the active-site residue of Escherichia coli aspartate aminotransferase (EC 2.6.1.1) that binds the substrate alpha-carboxylate, was replaced with tyrosine and phenylalanine by site-directed mutagenesis. This experiment was undertaken to elucidate the roles of particular enzyme-substrate interactions in triggering the substrate-induced conformational change in the enzyme. The activity and crystal structure of the resulting mutants were examined. The apparent second-order rate constants of both of these mutants are reduced by more than 5 orders of magnitude as compared to that of wild-type enzyme, though R386Y is slightly more active than R386F. The 2.5-A resolution structure of R386F in its native state was determined by using difference Fourier methods. The overall structure is very similar to that of the wild-type enzyme in the open conformation. The position of the Phe-386 side chain, however, appears to shift with respect to that of Arg-386 in the wild-type enzyme and to form new contacts with neighboring residues.


==About this Structure==
Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.,Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D Biochemistry. 1991 Feb 19;30(7):1980-5. PMID:1993208<ref>PMID:1993208</ref>
3AAT 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 SO4 and PLP 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=3AAT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase., Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D, Biochemistry. 1991 Feb 19;30(7):1980-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1993208 1993208]
</div>
[[Category: Aspartate transaminase]]
<div class="pdbe-citations 3aat" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Danishefsky, A.T.]]
[[Category: Danishefsky AT]]
[[Category: Petsko, G.A.]]
[[Category: Petsko GA]]
[[Category: Ringe, D.]]
[[Category: Ringe D]]
[[Category: PLP]]
[[Category: SO4]]
[[Category: transferase(aminotransferase)]]
 
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