The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit.

@article{Pas2008TheSO,
  title={The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit.},
  author={Gabriel Pa{\"e}s and Lars K. Skov and Michael J O'Donohue and Caroline R{\'e}mond and Jette Sandholm Kastrup and Michael Gajhede and Osman Mirza},
  journal={Biochemistry},
  year={2008},
  volume={47 28},
  pages={7441-51}
}
The crystal structure of the family GH-51 alpha- l-arabinofuranosidase from Thermobacillus xylanilyticus has been solved as a seleno-methionyl derivative. In addition, the structure of an inactive mutant Glu176Gln is presented in complex with a branched pentasaccharide, a fragment of its natural substrate xylan. The overall structure shows the two characteristic GH-51 domains: a catalytic domain that is folded into a (beta/alpha) 8-barrel and a C-terminal domain that displays jelly roll… CONTINUE READING