title: Structure of a feruloyl esterase from Aspergillus niger.
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.
authors.affiliation: CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, England.
authors.forename: Katherine E
authors.initials: KE
authors.lastname: McAuley
authors.forename: Allan
authors.initials: A
authors.lastname: Svendsen
authors.forename: Shamkant A
authors.initials: SA
authors.lastname: Patkar
authors.forename: Keith S
authors.initials: KS
authors.lastname: Wilson
mesh_terms: 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
chemical_list: 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