Publication Abstract from PubMed
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.
Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.,Rouvinen J, Bergfors T, Teeri T, Knowles JK, Jones TA Science. 1990 Jul 27;249(4967):380-6. PMID:2377893[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
