{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16(1)"],"submitter":["Li J"],"funding":["Li Jialu gratefully acknowledges support from the Sichuan Province Innovative Talent Funding Project for Postdoctoral Fellows","The Haihe Laboratory of Sustainable Chemical Transformations for financial support"],"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 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"],"journal":["Nature communications"],"pagination":["2054"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11871024"],"repository":["biostudies-literature"],"pubmed_title":["Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex."],"pmcid":["PMC11871024"],"pubmed_authors":["Liu H","Li H","Liu J","Li J","Zhu A","Dai X","Xiao Q","Qian W","Guo L","Deng D","Yan C","Luo Y","Wang X"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex.","description":"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","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-06-01T08:52:07.547Z","creation":"2025-04-07T11:28:20.008Z"},"accession":"S-EPMC11871024","cross_references":{"pubmed":["40021629"],"doi":["10.1038/s41467-025-57152-7"]}}