Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides

Maija-Liisa Mattinen, Markus Linder, Torbjörn Drakenberg, Arto Annila

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

The solution structure of a synthetic 38‐residue cellulose‐binding domain (CBD) of endoglucanase I from Trichoderma reesei (CBDEGI) was determined by two‐dimensional 1H‐NMR spectroscopy. 100 structures were generated from a total of 599 NOE derived distance restraints and 28 φ and 14 χ dihedral angle restraints.
For the final set of 19 selected structures, the rms deviation about the mean structure was 0.83 ± 0.26 Å for all atoms and 0.50 ± 0.22 Å for the backbone atoms. The structure of CBDEGI was very similar to that of CBD of cellobiohydrolase I from T. reesei (CBDCBHI). The backbone trace of CBDEGI followed closely the irregular triple‐stranded antiparallel β‐sheet structure of CBDCBHI. Moreover, apart from the different side chains of Trp7 (CBDEGI) and Tyr5 (CBDCBHI), the cellulose‐binding face of CBDEGI was similar to that of CBDCBHI within the precision of the structures.
Finally, the interaction between CBDEGI and soluble sugars was investigated using cellopentaose and cellohexaose as substrates. Experiments showed that the interactions between CBDEGI and cellobiose units of sugars are specific, supporting the previously presented model for the CBD binding to crystalline cellulose.

Original languageEnglish
Pages (from-to)279-286
JournalEuropean Journal of Biochemistry
Volume256
Issue number2
DOIs
Publication statusPublished - 1998
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Cellulases
Trichoderma
Oligosaccharides
Cellulose
Sugars
Cellobiose
Atoms
Dihedral angle
Spectrum Analysis
Spectroscopy
Crystalline materials
Substrates
Experiments

Cite this

Mattinen, Maija-Liisa ; Linder, Markus ; Drakenberg, Torbjörn ; Annila, Arto. / Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides. In: European Journal of Biochemistry. 1998 ; Vol. 256, No. 2. pp. 279-286.
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abstract = "The solution structure of a synthetic 38‐residue cellulose‐binding domain (CBD) of endoglucanase I from Trichoderma reesei (CBDEGI) was determined by two‐dimensional 1H‐NMR spectroscopy. 100 structures were generated from a total of 599 NOE derived distance restraints and 28 φ and 14 χ dihedral angle restraints. For the final set of 19 selected structures, the rms deviation about the mean structure was 0.83 ± 0.26 {\AA} for all atoms and 0.50 ± 0.22 {\AA} for the backbone atoms. The structure of CBDEGI was very similar to that of CBD of cellobiohydrolase I from T. reesei (CBDCBHI). The backbone trace of CBDEGI followed closely the irregular triple‐stranded antiparallel β‐sheet structure of CBDCBHI. Moreover, apart from the different side chains of Trp7 (CBDEGI) and Tyr5 (CBDCBHI), the cellulose‐binding face of CBDEGI was similar to that of CBDCBHI within the precision of the structures. Finally, the interaction between CBDEGI and soluble sugars was investigated using cellopentaose and cellohexaose as substrates. Experiments showed that the interactions between CBDEGI and cellobiose units of sugars are specific, supporting the previously presented model for the CBD binding to crystalline cellulose.",
author = "Maija-Liisa Mattinen and Markus Linder and Torbj{\"o}rn Drakenberg and Arto Annila",
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Solution structure of the cellulose-binding domain of endoglucanase I from Trichoderma reesei and its interaction with cello-oligosaccharides. / Mattinen, Maija-Liisa; Linder, Markus; Drakenberg, Torbjörn; Annila, Arto.

In: European Journal of Biochemistry, Vol. 256, No. 2, 1998, p. 279-286.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

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AB - The solution structure of a synthetic 38‐residue cellulose‐binding domain (CBD) of endoglucanase I from Trichoderma reesei (CBDEGI) was determined by two‐dimensional 1H‐NMR spectroscopy. 100 structures were generated from a total of 599 NOE derived distance restraints and 28 φ and 14 χ dihedral angle restraints. For the final set of 19 selected structures, the rms deviation about the mean structure was 0.83 ± 0.26 Å for all atoms and 0.50 ± 0.22 Å for the backbone atoms. The structure of CBDEGI was very similar to that of CBD of cellobiohydrolase I from T. reesei (CBDCBHI). The backbone trace of CBDEGI followed closely the irregular triple‐stranded antiparallel β‐sheet structure of CBDCBHI. Moreover, apart from the different side chains of Trp7 (CBDEGI) and Tyr5 (CBDCBHI), the cellulose‐binding face of CBDEGI was similar to that of CBDCBHI within the precision of the structures. Finally, the interaction between CBDEGI and soluble sugars was investigated using cellopentaose and cellohexaose as substrates. Experiments showed that the interactions between CBDEGI and cellobiose units of sugars are specific, supporting the previously presented model for the CBD binding to crystalline cellulose.

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