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

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 () and Xiang Wang ()
Additional contact information
Jialu Li: Sichuan University
Huayi Liu: Tianjin University
Jian Li: Tianjin University
Juxiu Liu: Sichuan University
Xinli Dai: Sichuan University
Angqi Zhu: Tsinghua University
Qingjie Xiao: Chinese Academy of Sciences
Wenyu Qian: Sichuan University
Honghao Li: Tianjin University
Li Guo: Sichuan University
Chuangye Yan: Tsinghua University
Dong Deng: Sichuan University
Yunzi Luo: Tianjin University
Xiang Wang: Sichuan University

Nature Communications, 2025, vol. 16, issue 1, 1-11

Abstract: 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.

Date: 2025
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-57152-7 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57152-7

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-57152-7

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().