1hix

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Image:1hix.gif

1hix, resolution 2.0Å

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CRYSTALLOGRAPHIC ANALYSES OF FAMILY 11 ENDO-BETA-1,4-XYLANASE XYL1 FROM STREPTOMYCES SP. S38

Overview

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.

About this Structure

1HIX is a Single protein structure of sequence from Streptomyces mobaraensis. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of family 11 endo-beta-1,4-xylanase Xyl1 from Streptomyces sp. S38., Wouters J, Georis J, Engher D, Vandenhaute J, Dusart J, Frere JM, Depiereux E, Charlier P, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1813-9. Epub 2001, Nov 21. PMID:11717493

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