Crystallographic analysis of family 11 endo-beta-1,4-xylanase Xyl1 from Streptomyces sp. S38.
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.
Wouters
J
J
Unité de Recherche en Biologie Moléculaire, Facultés Universitaires Notre Dame de la Paix, 61 Rue de Bruxelles, B-5000 Namur, Belgium. johan.wouters@fundp.ac.be
Georis
J
J
Engher
D
D
Vandenhaute
J
J
Dusart
J
J
Frere
J M
JM
Depiereux
E
E
Charlier
P
P
D000595:Amino Acid Sequence; D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D043364:Endo-1,4-beta Xylanases; D018698:Glutamic Acid / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013302:Streptomyces / Q000201:enzymology*; D014995:Xylosidases / Q000737:chemistry*
D018698:Glutamic Acid; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases; C121995:xyl1 xylanase