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Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.

Rouvinen J, Bergfors T, Teeri T, Knowles JK, Jones TA
Science 249 380-6 (1990)
Cited: 267 times
EuropePMC logo PMID: 2377893

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 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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  1. Genomic insights into the fungal lignocellulolytic system of Myceliophthora thermophila. Karnaouri A, Topakas E, Antonopoulou I, Christakopoulos P. Front Microbiol 5 281 (2014)

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