ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Family 11 endo-β-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 Å, γ = 120.0°. The structure was solved at 2.0 Å by X-ray crystallography using the molecular-replacement method and refined to a final R factor of 18.5% (Rfree = 26.9%). Xyl1 has the overall fold characteristic of family 11 xylanases, with two highly twisted β-sheets defining a long cleft containing the two catalytic residues Glu87 and Glu177.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444901015153
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