The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei

Christina Divne, Jerry Ståhlberg, Tapani Reinikainen, Laura Ruohonen, Göran Pettersson, Jonathan Knowles, Tuula Teeri, Alwyn Jones

Research output: Contribution to journalArticleScientificpeer-review

510 Citations (Scopus)

Abstract

Cellulose is the major polysaccharide of plants where it plays a predominantly structural role. A variety of highly specialized microorganisms have evolved to produce enzymes that either synergistically or in complexes can carry out the complete hydrolysis of cellulose. The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long active site tunnel that may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose. The active site residues were identified by solving the structure of the enzyme complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The three-dimensional structure is very similar to a family of bacterial beta-glucanases with the main-chain topology of the plant legume lectins.
Original languageEnglish
Pages (from-to)524-528
JournalScience
Volume265
Issue number5171
DOIs
Publication statusPublished - 1994
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Cellulose
Crystal structure
Enzymes
Plant Lectins
Fungi
Oligosaccharides
Microorganisms
Polysaccharides
Hydrolysis
Tunnels
Topology
Molecules

Cite this

Divne, C., Ståhlberg, J., Reinikainen, T., Ruohonen, L., Pettersson, G., Knowles, J., ... Jones, A. (1994). The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science, 265(5171), 524-528. https://doi.org/10.1126/science.8036495
Divne, Christina ; Ståhlberg, Jerry ; Reinikainen, Tapani ; Ruohonen, Laura ; Pettersson, Göran ; Knowles, Jonathan ; Teeri, Tuula ; Jones, Alwyn. / The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. In: Science. 1994 ; Vol. 265, No. 5171. pp. 524-528.
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title = "The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei",
abstract = "Cellulose is the major polysaccharide of plants where it plays a predominantly structural role. A variety of highly specialized microorganisms have evolved to produce enzymes that either synergistically or in complexes can carry out the complete hydrolysis of cellulose. The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long active site tunnel that may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose. The active site residues were identified by solving the structure of the enzyme complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The three-dimensional structure is very similar to a family of bacterial beta-glucanases with the main-chain topology of the plant legume lectins.",
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Divne, C, Ståhlberg, J, Reinikainen, T, Ruohonen, L, Pettersson, G, Knowles, J, Teeri, T & Jones, A 1994, 'The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei', Science, vol. 265, no. 5171, pp. 524-528. https://doi.org/10.1126/science.8036495

The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. / Divne, Christina; Ståhlberg, Jerry; Reinikainen, Tapani; Ruohonen, Laura; Pettersson, Göran; Knowles, Jonathan; Teeri, Tuula; Jones, Alwyn.

In: Science, Vol. 265, No. 5171, 1994, p. 524-528.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei

AU - Divne, Christina

AU - Ståhlberg, Jerry

AU - Reinikainen, Tapani

AU - Ruohonen, Laura

AU - Pettersson, Göran

AU - Knowles, Jonathan

AU - Teeri, Tuula

AU - Jones, Alwyn

N1 - Project code: BIO1004

PY - 1994

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N2 - Cellulose is the major polysaccharide of plants where it plays a predominantly structural role. A variety of highly specialized microorganisms have evolved to produce enzymes that either synergistically or in complexes can carry out the complete hydrolysis of cellulose. The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long active site tunnel that may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose. The active site residues were identified by solving the structure of the enzyme complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The three-dimensional structure is very similar to a family of bacterial beta-glucanases with the main-chain topology of the plant legume lectins.

AB - Cellulose is the major polysaccharide of plants where it plays a predominantly structural role. A variety of highly specialized microorganisms have evolved to produce enzymes that either synergistically or in complexes can carry out the complete hydrolysis of cellulose. The structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic fungus Trichoderma reesei has been determined and refined to 1.8 angstrom resolution. The molecule contains a 40 angstrom long active site tunnel that may account for many of the previously poorly understood macroscopic properties of the enzyme and its interaction with solid cellulose. The active site residues were identified by solving the structure of the enzyme complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The three-dimensional structure is very similar to a family of bacterial beta-glucanases with the main-chain topology of the plant legume lectins.

U2 - 10.1126/science.8036495

DO - 10.1126/science.8036495

M3 - Article

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JO - Science

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Divne C, Ståhlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles J et al. The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science. 1994;265(5171):524-528. https://doi.org/10.1126/science.8036495