Abstract
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 that may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose. The active site residues were identified by solving the structure of the enzyme complexed with an oligosaccharide, o -iodobenzyl-1-thio-β-cellobioside. The three-dimensional structure is very similar to a family of bacterial β-glucanases with the main-chain topology of the plant legume lectins.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 8:01 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 14, 2024, 11 p.m.) |
Indexed | 3 weeks, 6 days ago (July 28, 2025, 5:30 p.m.) |
Issued | 31 years, 1 month ago (July 22, 1994) |
Published | 31 years, 1 month ago (July 22, 1994) |
Published Print | 31 years, 1 month ago (July 22, 1994) |
@article{Divne_1994, title={The Three-Dimensional Crystal Structure of the Catalytic Core of Cellobiohydrolase I from Trichoderma reesei}, volume={265}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.8036495}, DOI={10.1126/science.8036495}, number={5171}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Divne, Christina and Ståhlberg, Jerry and Reinikainen, Tapani and Ruohonen, Laura and Pettersson, Göran and Knowles, Jonathan K. C. and Teeri, Tuula T. and Jones, T. Alwyn}, year={1994}, month=jul, pages={524–528} }