5M60
Chaetomium thermophilum beta-1-3-glucanase
Summary for 5M60
| Entry DOI | 10.2210/pdb5m60/pdb |
| Descriptor | Beta-1,3-glucanase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | cellulose, glucanase, fungus, thermostability, glucans, transferase |
| Biological source | Chaetomium thermophilum |
| Total number of polymer chains | 1 |
| Total formula weight | 83204.73 |
| Authors | Papageorgiou, A.C.,Chen, J.,Li, D. (deposition date: 2016-10-23, release date: 2017-05-17, Last modification date: 2024-10-09) |
| Primary citation | Papageorgiou, A.C.,Chen, J.,Li, D. Crystal structure and biological implications of a glycoside hydrolase family 55 beta-1,3-glucanase from Chaetomium thermophilum. Biochim. Biophys. Acta, 1865:1030-1038, 2017 Cited by PubMed Abstract: Crystal structures of a β-1,3-glucanase from the thermophilic fungus Chaetomium thermophilum were determined at 1.20 and 1.42Å resolution in the free and glucose-bound form, respectively. This is the third structure of a family 55 glycoside hydrolase (GH55) member and the second from a fungus. Based on comparative structural studies and site-directed mutagenesis, Glu654 is proposed as the catalytic acid residue. The substrate binding cleft exhibits restricted access on one side, rendering the enzyme as an exo-β-1,3-glucanase as confirmed also by thin layer chromatography experiments. A lack of stacking interactions was found at the substrate binding cleft, suggesting that interactions at positions -1, +1 and +2 are sufficient to orientate the substrate. A binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. PubMed: 28479293DOI: 10.1016/j.bbapap.2017.05.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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