Structure of xylanase Xys1Δ from Streptomyces halstedii

• Published in: Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-08, Vol.59 (8), p.1447-1453
• Main Authors: Canals, Albert, Vega, M. Cristina, Gomis-Rüth, F. Xavier, Díaz, Margarita, Santamaría, Ramón I., Coll, Miquel
• Format: Article
• Language: English
• Subjects: glycoside hydrolase family 10; TIM-barrel fold; xylan degradation; xylanases
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444903012629

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.