Three-Dimensional Structure of Cellobiohydrolase II from <i>Trichoderma reesei</i>

• J. Rouvinen

  Department of Molecular Biology, BMC, Uppsala, Sweden.

• T. Bergfors

  Department of Molecular Biology, BMC, Uppsala, Sweden.

• T. Teeri

  Biotechnical Laboratory, VIT, Espoo, Finland

• J. K. Knowles

  Biotechnical Laboratory, VIT, Espoo, Finland

• T. A. Jones

  Department of Molecular Biology, BMC, Uppsala, Sweden.

抄録

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.

収録刊行物

• Science

  Science 249 (4967), 380-386, 1990-07-27

  American Association for the Advancement of Science (AAAS)

キーワード

• Multidisciplinary

詳細情報

• CRID: 1363107370066283776
• NII論文ID: 80005454774
• DOI: 10.1126/science.2377893
• ISSN: 10959203
• ISSN: 00368075
• Web Site: https://www.science.org/doi/pdf/10.1126/science.2377893
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