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

517 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

Fingerprint

cellulose 1,4-beta-cellobiosidase
Trichoderma reesei
cellulose
triose-phosphate isomerase
aspartic acid
endo-1,4-beta-glucanase
active sites
topology
fungi
degradation
proteins

Cite this

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
Rouvinen, Juha ; Bergfors, Terese ; Teeri, Tuula ; Knowles, Jonathan ; Jones, Alwyn. / Three dimensional structure of cellobiohydrolase II from Trichoderma reesei. In: Science. 1990 ; Vol. 249, No. 4967. pp. 380-386.
@article{c6aab775b1db4f6a8aed1d4a033bfdf9,
title = "Three dimensional structure of cellobiohydrolase II from Trichoderma reesei",
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.",
author = "Juha Rouvinen and Terese Bergfors and Tuula Teeri and Jonathan Knowles and Alwyn Jones",
year = "1990",
doi = "10.1126/science.2377893",
language = "English",
volume = "249",
pages = "380--386",
journal = "Science",
issn = "0036-8075",
publisher = "American association for the advancement of science",
number = "4967",

}

Rouvinen, J, Bergfors, T, Teeri, T, Knowles, J & Jones, A 1990, 'Three dimensional structure of cellobiohydrolase II from Trichoderma reesei', Science, vol. 249, no. 4967, pp. 380-386. https://doi.org/10.1126/science.2377893

Three dimensional structure of cellobiohydrolase II from Trichoderma reesei. / Rouvinen, Juha; Bergfors, Terese; Teeri, Tuula; Knowles, Jonathan; Jones, Alwyn.

In: Science, Vol. 249, No. 4967, 1990, p. 380-386.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Three dimensional structure of cellobiohydrolase II from Trichoderma reesei

AU - Rouvinen, Juha

AU - Bergfors, Terese

AU - Teeri, Tuula

AU - Knowles, Jonathan

AU - Jones, Alwyn

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

U2 - 10.1126/science.2377893

DO - 10.1126/science.2377893

M3 - Article

VL - 249

SP - 380

EP - 386

JO - Science

JF - Science

SN - 0036-8075

IS - 4967

ER -

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