3tm7

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Current revision (10:10, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3tm7' size='340' side='right'caption='[[3tm7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3tm7' size='340' side='right'caption='[[3tm7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tm7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TM7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tm7]] is a 4 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=3TM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TM7 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=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]] 1.7&#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;'>[[1aw8|1aw8]], [[1ppy|1ppy]], [[1pqe|1pqe]], [[1pqf|1pqf]], [[1pqh|1pqh]], [[1pyq|1pyq]]</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=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">b0131, JW0127, panD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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_1-decarboxylase Aspartate 1-decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] </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=3tm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tm7 OCA], [https://pdbe.org/3tm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tm7 RCSB], [https://www.ebi.ac.uk/pdbsum/3tm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tm7 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=3tm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tm7 OCA], [https://pdbe.org/3tm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tm7 RCSB], [https://www.ebi.ac.uk/pdbsum/3tm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tm7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI]] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref>
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[https://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of the Asn72Ala site-directed mutant of Escherichia coli aspartate alpha-decarboxylase (ADC) has been determined at 1.7 A resolution. The refined structure is consistent with the presence of a hydrolysis product serine in the active site in place of the pyruvoyl group required for catalysis, which suggests that the role of Asn72 is to protect the ester formed during ADC activation from hydrolysis. In previously determined structures of activated ADC, including the wild type and other site-directed mutants, the C-terminal region of the protein is disordered, but in the Asn72Ala mutant these residues are ordered owing to an interaction with the active site of the neighbouring symmetry-related multimer.
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Structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation.,Webb ME, Lobley CM, Soliman F, Kilkenny ML, Smith AG, Blundell TL, Abell C Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):414-7. Epub, 2012 Mar 28. PMID:22505409<ref>PMID:22505409</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 3tm7" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspartate 1-decarboxylase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Ecoli]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Abell, C]]
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[[Category: Abell C]]
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[[Category: Blundell, T L]]
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[[Category: Blundell TL]]
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[[Category: Kilkenny, M L]]
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[[Category: Kilkenny ML]]
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[[Category: Lobley, C M.C]]
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[[Category: Lobley CMC]]
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[[Category: Smith, A G]]
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[[Category: Smith AG]]
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[[Category: Soliman, F]]
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[[Category: Soliman F]]
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[[Category: Webb, M E]]
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[[Category: Webb ME]]
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[[Category: Auto-processing]]
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[[Category: Lyase]]
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[[Category: Pyruvoyl]]
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Current revision

Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala

PDB ID 3tm7

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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