Bibliographic Details
| Title: |
Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex |
| 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 |
| Source: |
Nature Communications, Vol 16, Iss 1, Pp 1-11 (2025) |
| Publisher Information: |
Nature Portfolio, 2025. |
| Publication Year: |
2025 |
| Collection: |
LCC:Science |
| Subject Terms: |
Science |
| More Details: |
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. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
2041-1723 |
| Relation: |
https://doaj.org/toc/2041-1723 |
| DOI: |
10.1038/s41467-025-57152-7 |
| Access URL: |
https://doaj.org/article/677d5f6ac8cc434c9fd94c6943243576 |
| Accession Number: |
edsdoj.677d5f6ac8cc434c9fd94c6943243576 |
| Database: |
Directory of Open Access Journals |
