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Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma reesei

J. Rouvinen, T. Bergfors, T. Teeri, J. K. C. Knowles and T. A. Jones
Science
New Series, Vol. 249, No. 4967 (Jul. 27, 1990), pp. 380-386
Stable URL: http://www.jstor.org/stable/2874802
Page Count: 7
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Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma reesei
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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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