Structure of a feruloyl esterase from Aspergillus niger.
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.
McAuley
Katherine E
KE
CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, England.
Svendsen
Allan
A
Patkar
Shamkant A
SA
Wilson
Keith S
KS
D000595:Amino Acid Sequence; D001224:Aspartic Acid / Q000737:chemistry / Q000378:metabolism; D001234:Aspergillus niger / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D020134:Catalytic Domain; D003373:Coumaric Acids / Q000378:metabolism; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D006639:Histidine / Q000737:chemistry; D008049:Lipase / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000737:chemistry; D040681:Structural Homology, Protein
D001426:Bacterial Proteins; D003373:Coumaric Acids; D005656:Fungal Proteins; D001224:Aspartic Acid; D012694:Serine; D006639:Histidine; C004999:ferulic acid; D002265:Carboxylic Ester Hydrolases; D008049:Lipase; C070196:feruloyl esterase