Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex

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.

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Publication Details

Journal
Nature Communications
Published
2025-02-28
DOI
https://doi.org/10.1038/s41467-025-57152-7
Citations
16
Primary Topic
Signaling Pathways in Disease
Type
article
Field-Weighted Citation Impact
12.09
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article

Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex

Li Guo, Chuangye Yan, Angqi Zhu, Wen-Yu Qian et al.
16 citations
Nature Communications
Signaling Pathways in Disease
12.09
article

Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex

Li Guo, Chuangye Yan, Angqi Zhu, Wen-Yu Qian, Huayi Liu, Juxiu Liu, Yunzi Luo, Dong Deng, Jian Li, Xiang Wang, Xinli Dai, Qingjie Xiao, Honghao Li, Jialu Li
article en
16 citations

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 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.

Nature CommunicationsVol. 16(1)
Tianjin University (CN), Chinese Academy of Sciences (CN), Sichuan University (CN), West China Second University Hospital of Sichuan University (CN), Shanghai Advanced Research Institute (CN), Center for Life Sciences (CN), State Key Laboratory of Biotherapy, Tsinghua University (CN)
Openalex Percentile: Top 1%
Signaling Pathways in Disease
12.09
DOIOpen Access PDFOpenAlex
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