| Literature DB >> 11717493 |
J Wouters1, J Georis, D Engher, J Vandenhaute, J Dusart, J M Frere, E Depiereux, P Charlier.
Abstract
Family 11 endo-beta-1,4-xylanases degrade xylan, the main constituent of plant hemicelluloses, and have many potential uses in biotechnology. The structure of Xyl1, a family 11 endo-xylanase from Streptomyces sp. S38, has been solved. The protein crystallized from ammonium sulfate in the trigonal space group P321, with unit-cell parameters a = b = 71.49, c = 130.30 A, gamma = 120.0 degrees. The structure was solved at 2.0 A by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18.5% (R(free) = 26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with two highly twisted beta-sheets defining a long cleft containing the two catalytic residues Glu87 and Glu177.Entities:
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Year: 2001 PMID： 11717493 DOI： 10.1107/s0907444901015153
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN： 0907-4449