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- PDB-8wla: Cryo-EM structure of the beta-1,3-glucan synthase FKS1-Rho1 complex -

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Basic information

Entry
Database: PDB / ID: 8wla
TitleCryo-EM structure of the beta-1,3-glucan synthase FKS1-Rho1 complex
Components
  • 1,3-beta-glucan synthase component FKS1
  • GTP-binding protein RHO1
KeywordsMEMBRANE PROTEIN
Function / homology
Function and homology information


regulation of secondary cell septum biogenesis / PI3K/AKT activation / G beta:gamma signalling through PI3Kgamma / RHO GTPases activate PKNs / RND3 GTPase cycle / cellular bud neck septin ring organization / G alpha (12/13) signalling events / RHOF GTPase cycle / regulation of cell wall (1->3)-beta-D-glucan biosynthetic process / RND1 GTPase cycle ...regulation of secondary cell septum biogenesis / PI3K/AKT activation / G beta:gamma signalling through PI3Kgamma / RHO GTPases activate PKNs / RND3 GTPase cycle / cellular bud neck septin ring organization / G alpha (12/13) signalling events / RHOF GTPase cycle / regulation of cell wall (1->3)-beta-D-glucan biosynthetic process / RND1 GTPase cycle / positive regulation of mitotic actomyosin contractile ring assembly / fungal-type cell wall polysaccharide biosynthetic process / 1,3-beta-glucan synthase / 1,3-beta-D-glucan synthase activity / regulation of exocyst localization / : / RND2 GTPase cycle / (1->3)-beta-D-glucan biosynthetic process / budding cell bud growth / RHOC GTPase cycle / 1,3-beta-D-glucan synthase complex / regulation of fungal-type cell wall organization / spore wall / fungal-type cell wall biogenesis / regulation of vacuole fusion, non-autophagic / : / RHOA GTPase cycle / cellular bud / ascospore wall assembly / incipient cellular bud site / actin cortical patch / cellular bud tip / fungal-type cell wall / cellular bud neck / mating projection tip / fungal-type vacuole membrane / peroxisomal membrane / small GTPase-mediated signal transduction / regulation of cell size / positive regulation of endocytosis / Neutrophil degranulation / actin filament organization / small monomeric GTPase / cell periphery / regulation of actin cytoskeleton organization / enzyme activator activity / peroxisome / G-protein beta-subunit binding / regulation of protein localization / actin cytoskeleton organization / mitochondrial outer membrane / endosome membrane / GTPase activity / protein kinase binding / GTP binding / endoplasmic reticulum / Golgi apparatus / signal transduction / mitochondrion / membrane / plasma membrane / cytosol
Similarity search - Function
: / 1,3-beta-glucan synthase component FKS1, second domain / Glycosyl transferase, family 48 / 1,3-beta-glucan synthase subunit FKS1-like, domain-1 / 1,3-beta-glucan synthase component / 1,3-beta-glucan synthase subunit FKS1, domain-1 / 1,3-beta-glucan synthase subunit FKS1 / Small GTPase Rho / Small GTPase Rho domain profile. / Rho (Ras homology) subfamily of Ras-like small GTPases ...: / 1,3-beta-glucan synthase component FKS1, second domain / Glycosyl transferase, family 48 / 1,3-beta-glucan synthase subunit FKS1-like, domain-1 / 1,3-beta-glucan synthase component / 1,3-beta-glucan synthase subunit FKS1, domain-1 / 1,3-beta-glucan synthase subunit FKS1 / Small GTPase Rho / Small GTPase Rho domain profile. / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
GTP-binding protein RHO1 / 1,3-beta-glucan synthase component FKS1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsLi, J.L. / Zhu, A.Q. / Liu, J.X. / Dai, X.L. / Yan, C.Y. / Deng, D. / Wang, X.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Nat Commun / Year: 2025
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 /
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 ...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.
History
DepositionSep 29, 2023Deposition site: PDBJ / Processing site: PDBJ
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GTP-binding protein RHO1
B: 1,3-beta-glucan synthase component FKS1


Theoretical massNumber of molelcules
Total (without water)238,2662
Polymers238,2662
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein GTP-binding protein RHO1


Mass: 23189.445 Da / Num. of mol.: 1 / Mutation: Q68H
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: RHO1 / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P06780
#2: Protein 1,3-beta-glucan synthase component FKS1 / 1 / 3-beta-D-glucan-UDP glucosyltransferase / Calcineurin dependent protein 1 / Calcofluor white ...1 / 3-beta-D-glucan-UDP glucosyltransferase / Calcineurin dependent protein 1 / Calcofluor white hypersensitivity protein 53 / Echinocandin target gene protein 1 / FK506 sensitivity protein 1 / Glucan synthase of cerevisiae protein 1 / Papulacandin B resistance protein 1


Mass: 215076.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P38631, 1,3-beta-glucan synthase
Has ligand of interestN
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: 1,3-beta-glucan synthase component FKS1 in complex with GTPase Rho1
Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1100 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: NONE
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 93892 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00313779
ELECTRON MICROSCOPYf_angle_d0.52218717
ELECTRON MICROSCOPYf_dihedral_angle_d15.2034952
ELECTRON MICROSCOPYf_chiral_restr0.0382070
ELECTRON MICROSCOPYf_plane_restr0.0042380

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