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Title | Structure of a fungal 1,3-β-glucan synthase. |
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Journal, issue, pages | Sci Adv, Vol. 9, Issue 37, Page eadh7820, Year 2023 |
Publish date | Sep 15, 2023 |
Authors | Chao-Ran Zhao / Zi-Long You / Dan-Dan Chen / Jing Hang / Zhao-Bin Wang / Meng Ji / Le-Xuan Wang / Peng Zhao / Jie Qiao / Cai-Hong Yun / Lin Bai / |
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 ...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. |
External links | Sci Adv / PubMed:37703377 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.47 Å |
Structure data | EMDB-36748, PDB-8jzn: |
Chemicals | ChemComp-POV: ChemComp-AV0: ChemComp-ERG: |
Source |
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Keywords | TRANSFERASE / fungi / drug target |