8JZN
Structure of a fungal 1,3-beta-glucan synthase
Summary for 8JZN
| Entry DOI | 10.2210/pdb8jzn/pdb |
| EMDB information | 36748 |
| Descriptor | 1,3-beta-glucan synthase component FKS1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, ... (5 entities in total) |
| Functional Keywords | transferase, fungi, drug target |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 224584.16 |
| Authors | |
| Primary citation | Zhao, C.R.,You, Z.L.,Chen, D.D.,Hang, J.,Wang, Z.B.,Ji, M.,Wang, L.X.,Zhao, P.,Qiao, J.,Yun, C.H.,Bai, L. Structure of a fungal 1,3-beta-glucan synthase. Sci Adv, 9:eadh7820-eadh7820, 2023 Cited by PubMed Abstract: 1,3-β-Glucan serves as the primary component of the fungal cell wall and is produced by 1,3-β-glucan synthase located in the plasma membrane. This synthase is a molecular target for antifungal drugs such as echinocandins and the triterpenoid ibrexafungerp. In this study, we present the cryo-electron microscopy structure of 1,3-β-glucan synthase (Fks1) at 2.47-Å resolution. The structure reveals a central catalytic region adopting a cellulose synthase fold with a cytosolic conserved GT-A-type glycosyltransferase domain and a closed transmembrane channel responsible for glucan transportation. Two extracellular disulfide bonds are found to be crucial for Fks1 enzymatic activity. Through structural comparative analysis with cellulose synthases and structure-guided mutagenesis studies, we gain previously unknown insights into the molecular mechanisms of fungal 1,3-β-glucan synthase. PubMed: 37703377DOI: 10.1126/sciadv.adh7820 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.47 Å) |
Structure validation
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