3nad
From Proteopedia
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- | [[ | + | ==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=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3nad]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NAD FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
+ | <tr><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 Bacillus pumilus])</td></tr> | ||
+ | <tr><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://www.rcsb.org/pdb/explore.do?structureId=3nad RCSB], [http://www.ebi.ac.uk/pdbsum/3nad PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:21045284</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Bacillus pumilus]] | [[Category: Bacillus pumilus]] | ||
[[Category: Abokitse, K.]] | [[Category: Abokitse, K.]] |
Revision as of 10:26, 28 May 2014
Crystal Structure of Phenolic Acid Decarboxylase from Bacillus pumilus UI-670
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