Abstract
The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 A by molecular replacement. The protein has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the overall fold of the protein is very similar to that of the fungal lipases. The structure of the enzyme-product complex was determined to a resolution of 1.08 A and reveals dual conformations for the serine and histidine residues at the active site.
MeSH terms
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Amino Acid Sequence
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Aspartic Acid / chemistry
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Aspartic Acid / metabolism
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Aspergillus niger / enzymology*
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Binding Sites
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Carboxylic Ester Hydrolases / chemistry*
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Carboxylic Ester Hydrolases / metabolism*
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Catalytic Domain
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Coumaric Acids / metabolism
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Crystallography, X-Ray
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism
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Histidine / chemistry
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Lipase / chemistry
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Lipase / metabolism
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Sequence Homology, Amino Acid
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Serine / chemistry
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Structural Homology, Protein
Substances
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Bacterial Proteins
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Coumaric Acids
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Fungal Proteins
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Aspartic Acid
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Serine
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Histidine
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ferulic acid
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Carboxylic Ester Hydrolases
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Lipase
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feruloyl esterase