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Science 27 July 1990:
Vol. 249. no. 4967, pp. 380 - 386
DOI: 10.1126/science.2377893
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Articles

Science, Vol 249, Issue 4967, 380-386
Copyright © 1990 by American Association for the Advancement of Science

articles

Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei

J Rouvinen, T Bergfors, T Teeri, JK Knowles, and TA Jones

Department of Molecular Biology, BMC, Uppsala, Sweden.

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 alpha-beta 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 beta 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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