Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 60, Issue -, Pages 878-887Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444904004937
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The crystallographic structure of feruloyl esterase from Aspergillus niger has been determined to a resolution of 1.5 Angstrom 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 Angstrom and reveals dual conformations for the serine and histidine residues at the active site.
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