Source:http://linkedlifedata.com/resource/pubmed/id/21045284
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 11
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pubmed:dateCreated |
2010-11-3
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pubmed:databankReference | |
pubmed:abstractText |
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 ?-barrel structure and two ?-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 ?-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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1744-3091
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1407-14
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pubmed:meshHeading |
pubmed-meshheading:21045284-Amino Acid Sequence,
pubmed-meshheading:21045284-Bacillus,
pubmed-meshheading:21045284-Carboxy-Lyases,
pubmed-meshheading:21045284-Crystallography, X-Ray,
pubmed-meshheading:21045284-Models, Molecular,
pubmed-meshheading:21045284-Molecular Sequence Data,
pubmed-meshheading:21045284-Protein Structure, Quaternary,
pubmed-meshheading:21045284-Protein Structure, Tertiary,
pubmed-meshheading:21045284-Sequence Alignment
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pubmed:year |
2010
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pubmed:articleTitle |
Structural analysis of Bacillus pumilus phenolic acid decarboxylase, a lipocalin-fold enzyme.
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pubmed:affiliation |
Health Sector, Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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