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3pa9

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[[Image:3pa9.png|left|200px]]
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==Mechanism of inactivation of E. coli aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (S-ADFA) pH 7.5==
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<StructureSection load='3pa9' size='340' side='right' caption='[[3pa9]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3pa9]] 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=3PA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PA9 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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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3paa|3paa]]</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=3pa9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pa9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pa9 RCSB], [http://www.ebi.ac.uk/pdbsum/3pa9 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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{{STRUCTURE_3pa9| PDB=3pa9 | SCENE= }}
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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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===Mechanism of inactivation of E. coli aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (S-ADFA) pH 7.5===
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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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{{ABSTRACT_PUBMED_21033689}}
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==About this Structure==
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[[3pa9]] 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=3PA9 OCA].
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==See Also==
==See Also==
*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]
*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021033689</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Aspartate transaminase]]
[[Category: Aspartate transaminase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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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, R B]]
[[Category: Catalytic lysine]]
[[Category: Catalytic lysine]]
[[Category: Plp]]
[[Category: Plp]]

Revision as of 13:12, 9 December 2014

Mechanism of inactivation of E. coli aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid (S-ADFA) pH 7.5

3pa9, resolution 1.70Å

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