Structure of xylanase Xys1Δ from Streptomyces halstedii
Acta Crystallographica Section D
Volume 59, Issue 8, pages 1447–1453, August 2003
How to Cite
Canals, A., Vega, M. C., Gomis-Rüth, F. X., Díaz, M., Santamaría, R. I. and Coll, M. (2003), Structure of xylanase Xys1Δ from Streptomyces halstedii. Acta Crystallographica D, 59: 1447–1453. doi: 10.1107/S0907444903012629
- glycoside hydrolase family 10;
- xylan degradation;
- TIM-barrel fold.
Xylanases hydrolyze the β-1,4-linked xylose backbone of xylans. They are of increasing interest in the paper and food industries for their pre-bleaching and bio-pulping applications. Such industries demand new xylanases to cover a wider range of cleavage specificity, activity and stability. The catalytic domain of xylanase Xys1 from Streptomyces halstedii JM8 was expressed, purified and crystallized and native data were collected to 1.78 Å resolution with an Rmerge of 4.4%. The crystals belong to space group P212121, with unit-cell parameters a = 34.05, b = 79.60, c = 87.80 Å. The structure was solved by the molecular-replacement method using the structure of the homologue Xyl10A from Streptomyces lividans. In a similar manner to other members of its family, Xys1 folds to form a standard (β/α)8 barrel with the two catalytic functions, the acid/base and the nucleophile, at its C-terminal side. The overall structure is described and compared with those of related xylanases.