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

E Sabini, H Schubert, G Murshudov, K S Wilson, M Siika-Aho, M Penttilä

Journal: Acta crystallographica. Section D, Biological crystallography 2000;56(Pt 1):3-13

PMID: 10666621

Full Text on International Union of Crystallography View on PubMed

Abstract

The crystal structure of the catalytic core domain of beta-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 A. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P2(1). 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 beta-mannanase from the bacterium Thermomonospora fusca.

Address: Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, England.

DOI: 10.1107/s0907444999013943

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MeSH Terms: Actinomycetales, Amino Acid Sequence, Catalytic Domain, Crystallization, Crystallography, X-Ray, Glycoside Hydrolases, Hydrogen Bonding, Mannosidases, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Sequence Homology, Amino Acid, Static Electricity, Trichoderma, beta-Mannosidase