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- PDB-9op1: Cryo-EM structure of Candida albicans fluoride channel FEX in com... -

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Basic information

Entry
Database: PDB / ID: 9op1
TitleCryo-EM structure of Candida albicans fluoride channel FEX in complex with Fab fragment
Components
  • 10E8v4 Fab Heavy Chian
  • 10E8v4 Fab Light Chain
  • Transmembrane protein gp41,Fluoride export protein 1
KeywordsMEMBRANE PROTEIN / Fluoride channel / Fluoride exporter / FEX
Function / homology
Function and homology information


fluoride transmembrane transport / fluoride transmembrane transporter activity / Dectin-2 family / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane ...fluoride transmembrane transport / fluoride transmembrane transporter activity / Dectin-2 family / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / structural molecule activity / identical protein binding / membrane / plasma membrane
Similarity search - Function
Putative fluoride ion transporter CrcB / CrcB-like protein, Camphor Resistance (CrcB) / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120
Similarity search - Domain/homology
Envelope glycoprotein gp160 / Fluoride export protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
HIV-1 M:B_MN (virus)
Candida albicans SC5314 (yeast)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.05 Å
AuthorsKang, C.-Y. / An, M.J. / Ohi, M.D. / Stockbridge, R.B.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM128768 United States
CitationJournal: Nat Commun / Year: 2025
Title: The molecular mechanism of fluoride export by the eukaryotic fluoride channel FEX.
Authors: Chia-Yu Kang / Minjun An / Sahar Heidari / Hedieh Torabifard / Melanie D Ohi / Randy B Stockbridge /
Abstract: Much of life on Earth, including plants, fungi, and bacteria, evolved to resist toxic environmental fluoride. In eukaryotes, the major resistance mechanism is fluoride export by membrane proteins ...Much of life on Earth, including plants, fungi, and bacteria, evolved to resist toxic environmental fluoride. In eukaryotes, the major resistance mechanism is fluoride export by membrane proteins known as FEX. Using electrophysiology and transport assays, we establish that FEX from plants and yeasts are highly selective fluoride channels. Fluoride transport activity depends on reversible sodium ion binding, but sodium itself is not transported. We determine a structure of a FEX protein, from pathogenic yeast Candida albicans, using cryo-EM. Bolstered by mutagenesis studies, this structure reveals a fluoride permeation route through a single phenylalanine-lined pore. Molecular dynamics simulations demonstrate that a cation binding motif adjacent to the pore provides a stable sodium binding site that is accessible from the external aqueous solution. Comparison to the structurally related bacterial fluoride channels, Flucs, provides a glimpse of the evolution of structural and mechanistic complexity in a membrane protein family with inverted repeat architecture.
History
DepositionMay 16, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 3, 2025Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Dec 3, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Dec 24, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
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Revision 1.1Dec 24, 2025Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Database references / Experimental summary / Data content type: EM metadata / EM metadata / EM metadata / Category: citation / citation_author / em_admin
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 10E8v4 Fab Heavy Chian
B: 10E8v4 Fab Light Chain
C: Transmembrane protein gp41,Fluoride export protein 1


Theoretical massNumber of molelcules
Total (without water)86,3203
Polymers86,3203
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Antibody 10E8v4 Fab Heavy Chian


Mass: 25050.922 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): ExpiCHO-S cell line / Production host: Cricetulus griseus (Chinese hamster)
#2: Antibody 10E8v4 Fab Light Chain


Mass: 22458.945 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): ExpiCHO-S cell line / Production host: Cricetulus griseus (Chinese hamster)
#3: Protein Transmembrane protein gp41,Fluoride export protein 1 / TM / Glycoprotein 41 / gp41


Mass: 38810.254 Da / Num. of mol.: 1 / Fragment: residues 76-389,residues 76-389
Source method: isolated from a genetically manipulated source
Details: C. albicans Fluoride export protein 1, N-terminal epitope tag from HIV Transmembrane protein gp41,C. albicans Fluoride export protein 1, N-terminal epitope tag from HIV Transmembrane protein gp41
Source: (gene. exp.) HIV-1 M:B_MN (virus), (gene. exp.) Candida albicans SC5314 (yeast)
Strain: group M subtype B isolate MN, SC5314 / Gene: env, FEX1, CAALFM_C700270WA, CaO19.7095, orf19.7095 / Production host: Saccharomyces cerevisiae (brewer's yeast) / Strain (production host): BJ2168 / References: UniProt: P05877, UniProt: Q5AFH3
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

Component
IDNameTypeEntity IDParent-IDSource
1A complex of FEX with 10E8v4 FabCOMPLEXall0MULTIPLE SOURCES
2FEXCOMPLEX#31RECOMBINANT
310E8v4 FabCOMPLEX#1-#21RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-IDStrain
22Candida albicans (yeast)237561SC5314
33Homo sapiens (human)9606
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-IDStrainCell
22Saccharomyces cerevisiae (brewer's yeast)4932BJ2168
33Cricetulus griseus (Chinese hamster)10029ExpiCHO-S cell line
Buffer solutionpH: 7.5
Buffer component
IDConc.NameFormulaBuffer-ID
120 mMHEPESC8H18N2O4S1
2150 mMSodium ChlorideNaCl1
35 mMSodium FluorideNaF1
40.5 mMDDMC24H46O111
SpecimenConc.: 3.8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 291.15 K

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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 magnification: 105000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm
Specimen holderCryogen: NITROGEN
Image recordingAverage exposure time: 1.9 sec. / Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)
EM imaging opticsEnergyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV

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Processing

EM software
IDNameVersionCategory
2SerialEM4.1.1image acquisition
4cryoSPARC4.5CTF correction
7Coot0.9.8.93model fitting
9PHENIX1.21_5207model refinement
10cryoSPARC4.5initial Euler assignment
11cryoSPARC4.5final Euler assignment
13cryoSPARC4.53D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 4.05 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 164326 / Symmetry type: POINT
Atomic model building

3D fitting-ID: 1

IDPDB-IDChain-IDDetailsSource nameTypeAccession codeInitial refinement model-ID
1cUse AlphaFold2 to generate the FEX model.AlphaFoldin silico model
25IQ9

5iq9

PDBexperimental model5IQ92
RefinementHighest resolution: 4.05 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0035994
ELECTRON MICROSCOPYf_angle_d0.6298160
ELECTRON MICROSCOPYf_dihedral_angle_d4.52817
ELECTRON MICROSCOPYf_chiral_restr0.043925
ELECTRON MICROSCOPYf_plane_restr0.0051021

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