9R4L
Crystal structure of CtGH76 from Chaetomium thermophilum in complex with mannose
Summary for 9R4L
| Entry DOI | 10.2210/pdb9r4l/pdb |
| Descriptor | Chains: A, GLYCEROL, FORMIC ACID, ... (5 entities in total) |
| Functional Keywords | glycoside hydrolases, carbohydrate-binding protein, hydrolase |
| Biological source | Thermochaetoides thermophila DSM 1495 |
| Total number of polymer chains | 1 |
| Total formula weight | 48767.67 |
| Authors | Po-Hsun, W.,Essen, L.-O. (deposition date: 2025-05-07, release date: 2025-07-16, Last modification date: 2025-08-06) |
| Primary citation | Ruppenthal, S.R.,Po-Hsun, W.,Watad, M.,Rosner, C.J.,Vogt, M.S.,Friedrich, M.,Voigt, A.L.,Petz, A.,Gnau, P.,Essen, L.O. Ct GH76, a Glycoside Hydrolase 76 from Chaetomium thermophilum , with Elongated Glycan-Binding Canyon. Int J Mol Sci, 26:-, 2025 Cited by PubMed Abstract: Fungal cell walls, composed of polysaccharides and proteins, play critical roles in adaptation, cell division, and protection against environmental stress. Their polyglucan components are continuously remodeled by various types of glycosyl hydrolases (GHs) and transferases (GTs). In and other ascomycetes, enzymes of the subfamily, which belong as GTs to the GH76 family, cleave an α1,4 linkage between glucosamine and mannose to facilitate covalent linkage of GPI-anchored proteins to the cell wall's polyglucans. In contrast, the functions of other fungal GH76 subfamilies are not understood. We characterized GH76 from the sordariomycete , a member of the GH76 subfamily, revealing conserved structural features and functional divergence within the GH76 family. Notably, our structural characterization by X-ray crystallography combined with glycan fragment screening indicated that GH76 can recognize GPI-anchors like members of the subfamily but shows a broader promiscuity toward other glycans with central α1,6-mannobiose motifs due to the presence of an elongated glycan-binding . These findings provide new insights into GH76 enzyme diversity and fungal cell wall maturation. PubMed: 40724838DOI: 10.3390/ijms26146589 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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