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- EMDB-37614: Cryo-EM structure of the beta-1,3-glucan synthase FKS1-Rho1 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-37614
TitleCryo-EM structure of the beta-1,3-glucan synthase FKS1-Rho1 complex
Map data
Sample
  • Complex: 1,3-beta-glucan synthase component FKS1 in complex with GTPase Rho1
    • Protein or peptide: GTP-binding protein RHO1
    • Protein or peptide: 1,3-beta-glucan synthase component FKS1
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 / regulation of cell wall (1->3)-beta-D-glucan biosynthetic process / cellular bud neck septin ring organization / G alpha (12/13) signalling events / RHOF GTPase cycle / regulation of exocyst localization ...regulation of secondary cell septum biogenesis / PI3K/AKT activation / G beta:gamma signalling through PI3Kgamma / RHO GTPases activate PKNs / RND3 GTPase cycle / regulation of cell wall (1->3)-beta-D-glucan biosynthetic process / cellular bud neck septin ring organization / G alpha (12/13) signalling events / RHOF GTPase cycle / regulation of exocyst localization / fungal-type cell wall polysaccharide biosynthetic process / RND1 GTPase cycle / 1,3-beta-glucan synthase / 1,3-beta-D-glucan synthase activity / positive regulation of mitotic actomyosin contractile ring assembly / (1->3)-beta-D-glucan biosynthetic process / 1,3-beta-D-glucan synthase complex / RHOD GTPase cycle / RND2 GTPase cycle / budding cell bud growth / RHOC GTPase cycle / regulation of fungal-type cell wall organization / spore wall / fungal-type cell wall biogenesis / RHOB GTPase cycle / RHOA GTPase cycle / cellular bud / regulation of vacuole fusion, non-autophagic / ascospore wall assembly / incipient cellular bud site / cellular bud tip / actin cortical patch / 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 / enzyme activator activity / small monomeric GTPase / actin filament organization / cell periphery / regulation of actin cytoskeleton organization / 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 family 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 family 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)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsLi JL / Zhu AQ / Liu JX / Dai XL / Yan CY / Deng D / Wang X
Funding support China, 1 items
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, 2023-
Header (metadata) releaseFeb 19, 2025-
Map releaseFeb 19, 2025-
UpdateMar 12, 2025-
Current statusMar 12, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_37614.png

Downloads & links

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Map

FileDownload / File: emd_37614.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.09 Å/pix.
x 256 pix.
= 278.272 Å		1.09 Å/pix.
x 256 pix.
= 278.272 Å		1.09 Å/pix.
x 256 pix.
= 278.272 Å

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.087 Å
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Contour LevelBy AUTHOR: 0.229
Minimum - Maximum-1.3301085 - 1.9612911
Average (Standard dev.)0.00061952317 (±0.05361856)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 278.272 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_37614_msk_1.map
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Additional map: #1

Fileemd_37614_additional_1.map
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Half map: #2

Fileemd_37614_half_map_1.map
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Half map: #1

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Sample components

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Entire : 1,3-beta-glucan synthase component FKS1 in complex with GTPase Rho1

EntireName: 1,3-beta-glucan synthase component FKS1 in complex with GTPase Rho1
Components
  • Complex: 1,3-beta-glucan synthase component FKS1 in complex with GTPase Rho1
    • Protein or peptide: GTP-binding protein RHO1
    • Protein or peptide: 1,3-beta-glucan synthase component FKS1

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Supramolecule #1: 1,3-beta-glucan synthase component FKS1 in complex with GTPase Rho1

SupramoleculeName: 1,3-beta-glucan synthase component FKS1 in complex with GTPase Rho1
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: GTP-binding protein RHO1

MacromoleculeName: GTP-binding protein RHO1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 23.189445 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSQQVGNSIR RKLVIVGDGA CGKTCLLIVF SKGQFPEVYV PTVFENYVAD VEVDGRRVEL ALWDTAGHED YDRLRPLSYP DSNVVLICF SIDLPDSLEN VQEKWIAEVL HFCQGVPIIL VGCKVDLRND PQTIEQLRQE GQQPVTSQEG QSVADQIGAT G YYECSAKT ...String:
MSQQVGNSIR RKLVIVGDGA CGKTCLLIVF SKGQFPEVYV PTVFENYVAD VEVDGRRVEL ALWDTAGHED YDRLRPLSYP DSNVVLICF SIDLPDSLEN VQEKWIAEVL HFCQGVPIIL VGCKVDLRND PQTIEQLRQE GQQPVTSQEG QSVADQIGAT G YYECSAKT GYGVREVFEA ATRASLMGKS KTNGKAKKNT TEKKKKKCVL L

UniProtKB: GTP-binding protein RHO1

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Macromolecule #2: 1,3-beta-glucan synthase component FKS1

MacromoleculeName: 1,3-beta-glucan synthase component FKS1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: 1,3-beta-glucan synthase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 215.076156 KDa
SequenceString: MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ PPNESYDQDY TNGEYYGQPP NMAAQDGEN FSDFSSYGPP GTPGYDSYGG QYTASQMSYG EPNSSGTSTP IYGNYDPNAI AMALPNEPYP AWTADSQSPV S IEQIEDIF ...String:
MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ PPNESYDQDY TNGEYYGQPP NMAAQDGEN FSDFSSYGPP GTPGYDSYGG QYTASQMSYG EPNSSGTSTP IYGNYDPNAI AMALPNEPYP AWTADSQSPV S IEQIEDIF IDLTNRLGFQ RDSMRNMFDH FMVLLDSRSS RMSPDQALLS LHADYIGGDT ANYKKWYFAA QLDMDDEIGF RN MSLGKLS RKARKAKKKN KKAMEEANPE DTEETLNKIE GDNSLEAADF RWKAKMNQLS PLERVRHIAL YLLCWGEANQ VRF TAECLC FIYKCALDYL DSPLCQQRQE PMPEGDFLNR VITPIYHFIR NQVYEIVDGR FVKRERDHNK IVGYDDLNQL FWYP EGIAK IVLEDGTKLI ELPLEERYLR LGDVVWDDVF FKTYKETRTW LHLVTNFNRI WVMHISIFWM YFAYNSPTFY THNYQ QLVD NQPLAAYKWA SCALGGTVAS LIQIVATLCE WSFVPRKWAG AQHLSRRFWF LCIIFGINLG PIIFVFAYDK DTVYST AAH VVAAVMFFVA VATIIFFSIM PLGGLFTSYM KKSTRRYVAS QTFTAAFAPL HGLDRWMSYL VWVTVFAAKY SESYYFL VL SLRDPIRILS TTAMRCTGEY WWGAVLCKVQ PKIVLGLVIA TDFILFFLDT YLWYIIVNTI FSVGKSFYLG ISILTPWR N IFTRLPKRIY SKILATTDME IKYKPKVLIS QVWNAIIISM YREHLLAIDH VQKLLYHQVP SEIEGKRTLR APTFFVSQD DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVK DTKILAEETA AYEGNENEAE KEDALKSQID DLPFYCIGFK SAAPEYTLRT RIWASLRSQT LYRTISGFMN Y SRAIKLLY RVENPEIVQM FGGNAEGLER ELEKMARRKF KFLVSMQRLA KFKPHELENA EFLLRAYPDL QIAYLDEEPP LT EGEEPRI YSALIDGHCE ILDNGRRRPK FRVQLSGNPI LGDGKSDNQN HALIFYRGEY IQLIDANQDN YLEECLKIRS VLA EFEELN VEQVNPYAPG LRYEEQTTNH PVAIVGAREY IFSENSGVLG DVAAGKEQTF GTLFARTLSQ IGGKLHYGHP DFIN ATFMT TRGGVSKAQK GLHLNEDIYA GMNAMLRGGR IKHCEYYQCG KGRDLGFGTI LNFTTKIGAG MGEQMLSREY YYLGT QLPV DRFLTFYYAH PGFHLNNLFI QLSLQMFMLT LVNLSSLAHE SIMCIYDRNK PKTDVLVPIG CYNFQPAVDW VRRYTL SIF IVFWIAFVPI VVQELIERGL WKATQRFFCH LLSLSPMFEV FAGQIYSSAL LSDLAIGGAR YISTGRGFAT SRIPFSI LY SRFAGSAIYM GARSMLMLLF GTVAHWQAPL LWFWASLSSL IFAPFVFNPH QFAWEDFFLD YRDYIRWLSR GNNQYHRN S WIGYVRMSRA RITGFKRKLV GDESEKAAGD ASRAHRTNLI MAEIIPCAIY AAGCFIAFTF INAQTGVKTT DDDRVNSVL RIIICTLAPI AVNLGVLFFC MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA VIVHIAFFIV MWVLESFNFV RMLIGVVTCI QCQRLIFHC MTALMLTREF KNDHANTAFW TGKWYGKGMG YMAWTQPSRE LTAKVIELSE FAADFVLGHV ILICQLPLII I PKIDKFHS IMLFWLKPSR QIRPPIYSLK QTRLRKRMVK KYCSLYFLVL AIFAGCIIGP AVASAKIHKH IGDSLDGVVH NL FQPINTT NNDTGSQMST YQSHYYTHTP SLKTWSTIK

UniProtKB: 1,3-beta-glucan synthase component FKS1

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.1 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 93892
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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