The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.

@article{Divne1994TheTC,
  title={The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.},
  author={Christina Divne and Jerry St{\aa}hlberg and Tapani Reinikainen and Laura Ruohonen and Goran Pettersson and James K. Knowles and Tuula T. Teeri and T. A. Jones},
  journal={Science},
  year={1994},
  volume={265 5171},
  pages={524-8}
}
Cellulose is the major polysaccharide of plants where it plays a predominantly structural role. A variety of highly specialized microorganisms have evolved to produce enzymes that either synergistically or in complexes can carry out the complete hydrolysis of cellulose. The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long active site tunnel… CONTINUE READING
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