Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei

Maija-Liisa Mattinen (Corresponding Author), Maarit Kontteli, Janne Kerovuo, Markus Linder, Arto Annila, Gunnar Lindeberg, Tapani Reinikainen, Torbjörn Drakenberg

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Abstract

Three‐dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel β‐sheet structure of the CBD fold was preserved in all engineered peptides. The three‐dimensional NMR‐based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N‐terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.

Original languageEnglish
Pages (from-to)294 - 303
Number of pages10
JournalProtein Science
Volume6
Issue number2
DOIs
Publication statusPublished - 1997
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Trichoderma
Cellulose
Circular Dichroism
Circular dichroism spectroscopy
Dichroism
Spectrum Analysis
Polymers
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Crystalline materials
Glucose
Peptides
Mutation

Cite this

Mattinen, M-L., Kontteli, M., Kerovuo, J., Linder, M., Annila, A., Lindeberg, G., ... Drakenberg, T. (1997). Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei. Protein Science, 6(2), 294 - 303. https://doi.org/10.1002/pro.5560060204
Mattinen, Maija-Liisa ; Kontteli, Maarit ; Kerovuo, Janne ; Linder, Markus ; Annila, Arto ; Lindeberg, Gunnar ; Reinikainen, Tapani ; Drakenberg, Torbjörn. / Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei. In: Protein Science. 1997 ; Vol. 6, No. 2. pp. 294 - 303.
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abstract = "Three‐dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel β‐sheet structure of the CBD fold was preserved in all engineered peptides. The three‐dimensional NMR‐based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N‐terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.",
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Mattinen, M-L, Kontteli, M, Kerovuo, J, Linder, M, Annila, A, Lindeberg, G, Reinikainen, T & Drakenberg, T 1997, 'Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei', Protein Science, vol. 6, no. 2, pp. 294 - 303. https://doi.org/10.1002/pro.5560060204

Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei. / Mattinen, Maija-Liisa (Corresponding Author); Kontteli, Maarit; Kerovuo, Janne; Linder, Markus; Annila, Arto; Lindeberg, Gunnar; Reinikainen, Tapani; Drakenberg, Torbjörn.

In: Protein Science, Vol. 6, No. 2, 1997, p. 294 - 303.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei

AU - Mattinen, Maija-Liisa

AU - Kontteli, Maarit

AU - Kerovuo, Janne

AU - Linder, Markus

AU - Annila, Arto

AU - Lindeberg, Gunnar

AU - Reinikainen, Tapani

AU - Drakenberg, Torbjörn

PY - 1997

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N2 - Three‐dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel β‐sheet structure of the CBD fold was preserved in all engineered peptides. The three‐dimensional NMR‐based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N‐terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.

AB - Three‐dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel β‐sheet structure of the CBD fold was preserved in all engineered peptides. The three‐dimensional NMR‐based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N‐terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.

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SN - 0961-8368

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