The three-dimensional structure of a Trichoderma reesei β-mannanase from glycoside hydrolase family 5

Elisabetta Sabini, Heidi Schubert, Garib Murshudov, Keith S. Wilson, Matti Siika-Aho, Merja Penttilä

Research output: Contribution to journalArticleScientificpeer-review

97 Citations (Scopus)

Abstract

The crystal structure of the catalytic core domain of β-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 Å. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P21. The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous β-mannanase from the bacterium Thermomonospora fusca.

Original languageEnglish
Pages (from-to)3-13
Number of pages11
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number1
DOIs
Publication statusPublished - 1 Jan 2000
MoE publication typeA1 Journal article-refereed

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glucosides
Trichoderma
Glycoside Hydrolases
Catalytic Domain
fungi
heavy metals
Heavy Metals
Platinum
Fungi
bacteria
enzymes
Bacteria
platinum
Crystal structure
Scattering
crystal structure
Enzymes
scattering
mannobiose

Cite this

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title = "The three-dimensional structure of a Trichoderma reesei β-mannanase from glycoside hydrolase family 5",
abstract = "The crystal structure of the catalytic core domain of β-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 {\AA}. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P21. The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous β-mannanase from the bacterium Thermomonospora fusca.",
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The three-dimensional structure of a Trichoderma reesei β-mannanase from glycoside hydrolase family 5. / Sabini, Elisabetta; Schubert, Heidi; Murshudov, Garib; Wilson, Keith S.; Siika-Aho, Matti; Penttilä, Merja.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 56, No. 1, 01.01.2000, p. 3-13.

Research output: Contribution to journalArticleScientificpeer-review

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AB - The crystal structure of the catalytic core domain of β-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 Å. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P21. The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous β-mannanase from the bacterium Thermomonospora fusca.

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