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==Substrate Activation in Aspartate Aminotransferase==
==Substrate Activation in Aspartate Aminotransferase==
<StructureSection load='4dbc' size='340' side='right' caption='[[4dbc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='4dbc' size='340' side='right'caption='[[4dbc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dbc]] is a 1 chain structure with 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=4DBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBC FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dbc]] is a 1 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=4DBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DBC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3QP:(E)-N-{2-HYDROXY-3-METHYL-6-[(PHOSPHONOOXY)METHYL]BENZYLIDENE}-L-ASPARTIC+ACID'>3QP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3QP:(E)-N-{2-HYDROXY-3-METHYL-6-[(PHOSPHONOOXY)METHYL]BENZYLIDENE}-L-ASPARTIC+ACID'>3QP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbc OCA], [http://pdbe.org/4dbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dbc RCSB], [http://www.ebi.ac.uk/pdbsum/4dbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbc ProSAT]</span></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=4dbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbc OCA], [https://pdbe.org/4dbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dbc RCSB], [https://www.ebi.ac.uk/pdbsum/4dbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbc ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the Calpha-H bond.
 
Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.,Griswold WR, Castro JN, Fisher AJ, Toney MD J Am Chem Soc. 2012 May 23;134(20):8436-8. doi: 10.1021/ja302809e. Epub 2012 May , 10. PMID:22551424<ref>PMID:22551424</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dbc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspartate transaminase]]
[[Category: Escherichia coli K-12]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Fisher, A J]]
[[Category: Fisher AJ]]
[[Category: Griswold, W R]]
[[Category: Griswold WR]]
[[Category: Toney, M D]]
[[Category: Toney MD]]
[[Category: Aminotransferase]]
[[Category: Transferase]]
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