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5ls7

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Current revision (18:44, 18 October 2023) (edit) (undo)
 
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<StructureSection load='5ls7' size='340' side='right'caption='[[5ls7]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
<StructureSection load='5ls7' size='340' side='right'caption='[[5ls7]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ls7]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LS7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LS7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ls7]] is a 3 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=5LS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LS7 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=74C:methyl+radical'>74C</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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]] 1.16&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=PVO:'>PVO</scene></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=74C:methyl+radical'>74C</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PVO:2,2-bis(oxidanyl)propanoic+acid'>PVO</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></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_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://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=5ls7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ls7 OCA], [https://pdbe.org/5ls7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ls7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ls7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ls7 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ls7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ls7 OCA], [http://pdbe.org/5ls7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ls7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ls7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ls7 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI]] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref> [[http://www.uniprot.org/uniprot/PANZ_ECOLI PANZ_ECOLI]] Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD (PubMed:23170229, PubMed:25910242). Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA (PubMed:25910242).<ref>PMID:23170229</ref> <ref>PMID:25910242</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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Monteiro, D C.F]]
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[[Category: Monteiro DCF]]
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[[Category: Pearson, A R]]
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[[Category: Pearson AR]]
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[[Category: Webb, M E]]
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[[Category: Webb ME]]
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[[Category: Coenzyme a biosynthesis]]
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[[Category: Lyase]]
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[[Category: Metabolic pathway regulation]]
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[[Category: Protein complex]]
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[[Category: Protein derived cofactor]]
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Current revision

Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ

PDB ID 5ls7

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