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Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex
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Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex
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Journal Article
Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex
2025
Overview
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.
Cryo-EM structures of apo-FKS1 and the FKS1-Rho1 complex reveal how Rho1 activates FKS1, driving conformational changes of FKS1 in β−1,3- glucan synthesis.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Fungal Proteins - metabolism
/ Fungal Proteins - ultrastructure
/ Glucan
/ Glucose
/ Glucosyltransferases - chemistry
/ Glucosyltransferases - genetics
/ Glucosyltransferases - metabolism
/ Glucosyltransferases - ultrastructure
/ Humanities and Social Sciences
/ Proteins
/ rho GTP-Binding Proteins - chemistry
/ rho GTP-Binding Proteins - genetics
/ rho GTP-Binding Proteins - metabolism
/ rho GTP-Binding Proteins - ultrastructure
/ Science
/ Yeast
