Three-Dimensional Structure of Cellobiohydrolase II from <i>Trichoderma reesei</i>
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- J. Rouvinen
- Department of Molecular Biology, BMC, Uppsala, Sweden.
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- T. Bergfors
- Department of Molecular Biology, BMC, Uppsala, Sweden.
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- T. Teeri
- Biotechnical Laboratory, VIT, Espoo, Finland
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- J. K. Knowles
- Biotechnical Laboratory, VIT, Espoo, Finland
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- T. A. Jones
- Department of Molecular Biology, BMC, Uppsala, Sweden.
抄録
<jats:p> 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 <jats:italic>Trichoderma reesei</jats:italic> 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. </jats:p>
収録刊行物
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- Science
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Science 249 (4967), 380-386, 1990-07-27
American Association for the Advancement of Science (AAAS)
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詳細情報 詳細情報について
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- CRID
- 1363107370066283776
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- NII論文ID
- 80005454774
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- ISSN
- 10959203
- 00368075
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- データソース種別
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