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    Science. 1990 Jul 27;249(4967):380-6.

    Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei.

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

    Source

    Department of Molecular Biology, BMC, Uppsala, Sweden.

    Erratum in

    • Science 1990 Sep 21;249(4975):1359.

    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.

    PMID:
    2377893
    [PubMed - indexed for MEDLINE]

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