[en] 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.
Joseleau J.P., Comptat J., Ruel K. Xylans and Xylanases , edited by J. Visser, G. Beldman, M. A. Kusters-Van Someren & A. G. J. Voragen. Amsterdam: Elsevier; 1992, 1-15.
Joshi M.D., Sidhu G., Pot I., Brayer G.D., Withers S.G., McIntosh L.P. J. Mol. Biol. 2000, 299:255-279.
Kraulis P.J. J. Appl. Cryst. 1991, 24:946-950.
Krengel U., Dijkstra B. J. Mol. Biol. 1996, 263:70-78.
Kumar P.R., Eswaramoorthy S., Vuthayathil P.J., Viswamitra M.A. J. Mol. Biol. 2000, 295:581-593.
