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Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma reesei

Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J. K., Jones, T. A.·1990·Science

Abstract

The enzymatic degradation of cellulose is an important process, both ecologically and commercially. The three-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus Trichoderma reesei reveals an α-β protein with a fold similar to but different from the widely occurring barrel topology first observed in triose phosphate isomerase. The active site of CBHII is located at the carboxyl-terminal end of a parallel β barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the center of the tunnel are the probable catalytic residues.

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Metadata

Authors
Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J. K., & Jones, T. A.
Venue
Science
Published
1990-07-27
Volume
249
Issue
4967
Pages
380-386
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2015478270
Cited by
606
References
0
FWCI
29.91
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma reesei. https://app.cochat.ai/papers/10.1126/science.2377893
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Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J. K., & Jones, T. A. (1990). Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma reesei. Science. https://doi.org/10.1126/science.2377893

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.