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| | ==Crystal Structure of Phenolic Acid Decarboxylase from Bacillus pumilus UI-670== | | ==Crystal Structure of Phenolic Acid Decarboxylase from Bacillus pumilus UI-670== |
| - | <StructureSection load='3nad' size='340' side='right' caption='[[3nad]], [[Resolution|resolution]] 1.69Å' scene=''> | + | <StructureSection load='3nad' size='340' side='right'caption='[[3nad]], [[Resolution|resolution]] 1.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_7061 Atcc 7061]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NAD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NAD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nad]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NAD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.69Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fdc, padC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1408 ATCC 7061])</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> |
| - | <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=3nad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nad OCA], [http://pdbe.org/3nad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nad RCSB], [http://www.ebi.ac.uk/pdbsum/3nad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nad 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=3nad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nad OCA], [https://pdbe.org/3nad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nad RCSB], [https://www.ebi.ac.uk/pdbsum/3nad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nad ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q45361_BACPU Q45361_BACPU] |
| | <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> |
| - | [[Category: Atcc 7061]] | + | [[Category: Bacillus pumilus]] |
| - | [[Category: Abokitse, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Bergeron, H]] | + | [[Category: Abokitse K]] |
| - | [[Category: Grosse, S]] | + | [[Category: Bergeron H]] |
| - | [[Category: Lau, P C.K]] | + | [[Category: Grosse S]] |
| - | [[Category: Matte, A]] | + | [[Category: Lau PCK]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Matte A]] |
| - | [[Category: Biocatalysis]]
| + | |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lipocalin]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q45361_BACPU
Publication Abstract from PubMed
The decarboxylation of phenolic acids, including ferulic and p-coumaric acids, to their corresponding vinyl derivatives is of importance in the flavouring and polymer industries. Here, the crystal structure of phenolic acid decarboxylase (PAD) from Bacillus pumilus strain UI-670 is reported. The enzyme is a 161-residue polypeptide that forms dimers both in the crystal and in solution. The structure of PAD as determined by X-ray crystallography revealed a beta-barrel structure and two alpha-helices, with a cleft formed at one edge of the barrel. The PAD structure resembles those of the lipocalin-fold proteins, which often bind hydrophobic ligands. Superposition of structurally related proteins bound to their cognate ligands shows that they and PAD bind their ligands in a conserved location within the beta-barrel. Analysis of the residue-conservation pattern for PAD-related sequences mapped onto the PAD structure reveals that the conservation mainly includes residues found within the hydrophobic core of the protein, defining a common lipocalin-like fold for this enzyme family. A narrow cleft containing several conserved amino acids was observed as a structural feature and a potential ligand-binding site.
Structural analysis of Bacillus pumilus phenolic acid decarboxylase, a lipocalin-fold enzyme.,Matte A, Grosse S, Bergeron H, Abokitse K, Lau PC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1407-14. Epub 2010 Oct 27. PMID:21045284[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matte A, Grosse S, Bergeron H, Abokitse K, Lau PC. Structural analysis of Bacillus pumilus phenolic acid decarboxylase, a lipocalin-fold enzyme. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1407-14. Epub 2010 Oct 27. PMID:21045284 doi:10.1107/S174430911003246X
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