Three dimensional structure of cellobiohydrolase II from Trichoderma reesei

Juha Rouvinen, Terese Bergfors, Tuula Teeri, Jonathan Knowles, Alwyn Jones

Research output: Contribution to journalArticleScientificpeer-review

527 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)380-386
JournalScience
Volume249
Issue number4967
DOIs
Publication statusPublished - 1990
MoE publication typeA1 Journal article-refereed

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    Rouvinen, J., Bergfors, T., Teeri, T., Knowles, J., & Jones, A. (1990). Three dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science, 249(4967), 380-386. https://doi.org/10.1126/science.2377893