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| | <StructureSection load='1qzu' size='340' side='right'caption='[[1qzu]], [[Resolution|resolution]] 2.91Å' scene=''> | | <StructureSection load='1qzu' size='340' side='right'caption='[[1qzu]], [[Resolution|resolution]] 2.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qzu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QZU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qzu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.91Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coac ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopantothenoylcysteine_decarboxylase Phosphopantothenoylcysteine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.36 4.1.1.36] </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=1qzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzu OCA], [https://pdbe.org/1qzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qzu RCSB], [https://www.ebi.ac.uk/pdbsum/1qzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzu OCA], [http://pdbe.org/1qzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qzu RCSB], [http://www.ebi.ac.uk/pdbsum/1qzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COAC_HUMAN COAC_HUMAN]] Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine.<ref>PMID:11923312</ref> <ref>PMID:15581364</ref> | + | [https://www.uniprot.org/uniprot/COAC_HUMAN COAC_HUMAN] Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine.<ref>PMID:11923312</ref> <ref>PMID:15581364</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphopantothenoylcysteine decarboxylase]]
| + | [[Category: Ealick SE]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Manoj N]] |
| - | [[Category: Manoj, N]] | + | |
| - | [[Category: Alpha-beta sandwich]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
COAC_HUMAN Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Phosphopantothenoylcysteine (PPC) decarboxylase is an essential enzyme in the biosynthesis of coenzyme A and catalyzes the decarboxylation of PPC to phosphopantetheine. Human PPC decarboxylase has been expressed in Escherichia coli, purified and crystallized. The Laue class of the diffraction data appears to be 3m, suggesting space group R32 with two monomers per asymmetric unit. However, the crystals belong to the space group R3 and the asymmetric unit contains four monomers. The structure has been solved using molecular replacement and refined to a current R factor of 29%. The crystal packing can be considered as two interlaced lattices, each consistent with space group R32 and with the corresponding twofold axes parallel to each other but separated along the threefold axis. Thus, the true space group is R3 with four monomers per asymmetric unit.
Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase.,Manoj N, Ealick SE Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1762-6. Epub 2003, Sep 19. PMID:14501115[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A. Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J Biol Chem. 2002 Jun 14;277(24):21431-9. Epub 2002 Mar 28. PMID:11923312 doi:http://dx.doi.org/10.1074/jbc.M201708200
- ↑ Strauss E, Zhai H, Brand LA, McLafferty FW, Begley TP. Mechanistic studies on phosphopantothenoylcysteine decarboxylase: trapping of an enethiolate intermediate with a mechanism-based inactivating agent. Biochemistry. 2004 Dec 14;43(49):15520-33. PMID:15581364 doi:http://dx.doi.org/10.1021/bi048340a
- ↑ Manoj N, Ealick SE. Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase. Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1762-6. Epub 2003, Sep 19. PMID:14501115
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