1HIX

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

Summary for 1HIX

• Entry DOI: 10.2210/pdb1hix/pdb
• Descriptor: ENDO-1,4-BETA-XYLANASE (2 entities in total)
• Functional Keywords: hydrolase, xylan degradation
• Biological source: STREPTOMYCES SP. S38
• Total number of polymer chains: 2
• Total formula weight: 41194.42

Authors

Wouters, J.,Georis, J.,Dusart, J.,Frere, J.M.,Depiereux, E.,Charlier, P. (deposition date: 2001-01-05, release date: 2001-11-30, Last modification date: 2023-12-13)

Primary citation

Wouters, J.,Georis, J.,Engher, D.,Vandenhaute, J.,Dusart, J.,Frere, J.M.,Depiereux, E.,Charlier, P.
Crystallographic Analysis of Family 11 Endo-[Beta]-1,4-Xylanase Xyl1 from Streptomyces Sp. S38
Acta Crystallogr.,Sect.D, 57:1813-, 2001

PubMed 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.

PubMed: 11717493
DOI: 10.1107/S0907444901015153

Experimental method

X-RAY DIFFRACTION (2 Å)