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3paa

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<StructureSection load='3paa' size='340' side='right'caption='[[3paa]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3paa' size='340' side='right'caption='[[3paa]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3paa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PAA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PAA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3paa]] 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=3PAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PAA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PJ7:4-AMINOFURAN-2-CARBOXYLIC+ACID'>PJ7</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pa9|3pa9]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PJ7:4-AMINOFURAN-2-CARBOXYLIC+ACID'>PJ7</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aspC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3paa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3paa OCA], [https://pdbe.org/3paa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3paa RCSB], [https://www.ebi.ac.uk/pdbsum/3paa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3paa ProSAT]</span></td></tr>
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<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>
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<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=3paa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3paa OCA], [http://pdbe.org/3paa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3paa RCSB], [http://www.ebi.ac.uk/pdbsum/3paa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3paa ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D3H0F7_ECO44 D3H0F7_ECO44]
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As a potential drug to treat neurological diseases, the mechanism-based inhibitor (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (S-ADFA) has been found to inhibit the gamma-aminobutyric acid aminotransferase (GABA-AT) reaction. To circumvent the difficulties in structural studies of a S-ADFA-enzyme complex using GABA-AT, l-aspartate aminotransferase (l-AspAT) from Escherichia coli was used as a model PLP-dependent enzyme. Crystal structures of the E. coli aspartate aminotransferase with S-ADFA bound to the active site were obtained via cocrystallization at pH 7.5 and 8. The complex structures suggest that S-ADFA inhibits the transamination reaction by forming adducts with the catalytic lysine 246 via a covalent bond while producing 1 equiv of pyridoxamine 5'-phosphate (PMP). Based on the structures, formation of the K246-S-ADFA adducts requires a specific initial binding configuration of S-ADFA in the l-AspAT active site, as well as deprotonation of the epsilon-amino group of lysine 246 after the formation of the quinonoid and/or ketimine intermediate in the overall inactivation reaction.
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Mechanism of Inactivation of Escherichia coli Aspartate Aminotransferase by (S)-4-Amino-4,5-dihydro-2-furancarboxylic Acid .,Liu D, Pozharski E, Fu M, Silverman RB, Ringe D Biochemistry. 2010 Nov 15. PMID:21033689<ref>PMID:21033689</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3paa" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Aspartate transaminase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fu, M]]
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[[Category: Fu M]]
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[[Category: Liu, D]]
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[[Category: Liu D]]
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[[Category: Pozharski, E]]
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[[Category: Pozharski E]]
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[[Category: Ringe, D]]
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[[Category: Ringe D]]
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[[Category: Silverman, R B]]
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[[Category: Silverman RB]]
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[[Category: Pmp]]
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[[Category: Sadfa]]
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[[Category: Transferase]]
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Current revision

Mechanism of inactivation of E. coli aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (S-ADFA) pH 8.0

PDB ID 3paa

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