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| Title | Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 2054, Year 2025 |
| Publish date | Feb 28, 2025 |
 Authors | Jialu Li / Huayi Liu / Jian Li / Juxiu Liu / Xinli Dai / Angqi Zhu / Qingjie Xiao / Wenyu Qian / Honghao Li / Li Guo / Chuangye Yan / Dong Deng / Yunzi Luo / Xiang Wang /  |
| PubMed Abstract | β-1,3 Glucan synthase (GS) is essential for fungal cell wall biosynthesis. The GS holoenzyme comprises the glycosyltransferase FKS1 and its regulatory factor Rho1, a small GTPase. However, the ...β-1,3 Glucan synthase (GS) is essential for fungal cell wall biosynthesis. The GS holoenzyme comprises the glycosyltransferase FKS1 and its regulatory factor Rho1, a small GTPase. However, the mechanism by which Rho1 activates FKS1 in a GTP-dependent manner remains unclear. Here, we present two cryo-EM structures of FKS1, apo and in complex with Rho1. FKS1 adopts a cellulose synthase-like conformation. The interaction between Rho1 and FKS1 is enhanced in the presence of GTPγS. Rho1 is positioned within a pocket between the glycosyltransferase domain of FKS1 (GT domain) and the transmembrane helix spanning TM7-15. Comparison of the two structures reveals extensive conformational changes within FKS1. These alterations suggest that Rho1's GTP/GDP cycling may act as a molecular pump, promoting a dynamic transition between the resting and active states of FKS1. Notably, Rho1 triggers FKS1 conformational changes that may push the growing glucan chain into FKS1's transmembrane channel, thereby facilitating β-1,3-glucan elongation. |
 External links | Nat Commun / PubMed:40021629 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.16 - 3.4 Å |
| Structure data | EMDB-37612, PDB-8wl6: EMDB-37614, PDB-8wla: |
| Source |
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 Keywords | MEMBRANE PROTEIN |
saccharomyces cerevisiae (brewer's yeast)