β-1,3-xylanase (1,3-β-D-xylan xylanohydrolase; EC 220.127.116.11) is an enzyme capable of hydrolyzing β-1,3-xylan. The newly cloned β-1,3-xylanase from the marine bacterium Vibrio sp. AX-4 (XYL4) exhibited a modular structure consisting of three modules: an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two C-terminal xylan-binding modules belonging to carbohydrate-binding module family 31. Despite substantial crystallization screening, crystallization of the recombinant XYL4 was not accomplished. However, the deletion mutant of XYL4, composed of a catalytic module without a xylan-binding module, was crystallized. The crystal belonged to space group P212121, with unit-cell parameters a = 51.6, b = 75.8, c = 82.0 Å. X-ray diffraction data were collected to 1.44 Å resolution.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - Aug 1 2004|
All Science Journal Classification (ASJC) codes
- Structural Biology