3qpg

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<StructureSection load='3qpg' size='340' side='right'caption='[[3qpg]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
<StructureSection load='3qpg' size='340' side='right'caption='[[3qpg]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qpg]] is a 1 chain structure with sequence from [https://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=3QPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qpg]] 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=3QPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPG FirstGlance]. <br>
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</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.79&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qn6|3qn6]]</div></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=3QP:(E)-N-{2-HYDROXY-3-METHYL-6-[(PHOSPHONOOXY)METHYL]BENZYLIDENE}-L-ASPARTIC+ACID'>3QP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3qpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpg OCA], [https://pdbe.org/3qpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpg RCSB], [https://www.ebi.ac.uk/pdbsum/3qpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpg 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=3qpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpg OCA], [https://pdbe.org/3qpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpg RCSB], [https://www.ebi.ac.uk/pdbsum/3qpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpg ProSAT]</span></td></tr>
</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/AAT_ECOLI AAT_ECOLI]
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The 1.8 A resolution crystal structures of Escherichia coli aspartate aminotransferase reconstituted with 1-deazapyridoxal 5'-phosphate (deazaPLP; 2-formyl-3-hydroxy-4-methylbenzyl phosphate) in the internal aldimine and l-aspartate external aldimine forms are reported. The l-aspartate.deazaPLP external aldimine is extraordinarily stable (half-life of &gt;20 days), allowing crystals of this intermediate to be grown by cocrystallization with l-aspartate. This structure is compared to that of the alpha-methyl-l-aspartate.PLP external aldimine. Overlays with the corresponding pyridoxal 5'-phosphate (PLP) aldimines show very similar orientations of deazaPLP with respect to PLP. The lack of a hydrogen bond between Asp222 and deazaPLP, which serves to "anchor" PLP in the active site, releases strain in the deazaPLP internal aldimine that is enforced in the PLP internal aldimine [Hayashi, H., Mizuguchi, H., Miyahara, I., Islam, M. M., Ikushiro, H., Nakajima, Y., Hirotsu, K., and Kagamiyama, H. (2003) Biochim. Biophys. Acta1647, 103] as evidenced by the planarity of the pyridine ring and the Schiff base linkage with Lys258. Additionally, loss of this anchor causes a 10 degrees greater tilt of deazaPLP toward the substrate in the external aldimine. An important mechanistic difference between the l-aspartate.deazaPLP and alpha-methyl-l-aspartate.PLP external aldimines is a hydrogen bond between Gly38 and Lys258 in the former, positioning the catalytic base above and approximately equidistant between Calpha and C4'. In contrast, in the alpha-methyl-l-aspartate.PLP external aldimine, the epsilon-amino group of Lys258 is rotated approximately 70 degrees to form a hydrogen bond to Tyr70 because of the steric bulk of the methyl group.
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Crystal Structures of Aspartate Aminotransferase Reconstituted with 1-Deazapyridoxal 5'-Phosphate: Internal Aldimine and Stable l-Aspartate External Aldimine.,Griswold WR, Fisher AJ, Toney MD Biochemistry. 2011 Jun 9. PMID:21627105<ref>PMID:21627105</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 3qpg" 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: Griswold, W R]]
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[[Category: Griswold WR]]
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[[Category: Aminotransferase]]
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[[Category: Transferase]]
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Current revision

Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with 1-Deaza-Pyridoxal 5'-Phosphate: Internal Aldimine and Stable L-Aspartate External Aldimine

PDB ID 3qpg

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