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- EMDB-72248: KCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and ca... -

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Basic information

Entry
Database: EMDB / ID: EMD-72248
TitleKCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and calmodulin
Map dataKCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and calmodulin
Sample
  • Complex: KCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and calmodulin
KeywordsVoltage gated potassium channel / cardiac / fluorinated phenylalanine / MEMBRANE PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.43 Å
AuthorsSchene ME / Ahern CA
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2026
Title: Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the K7.1 potassium channel.
Authors: Miranda E Schene / Christopher A Ahern /
Abstract: K7.1 is a cardiac voltage-gated potassium channel that underlies the delayed rectifier current (I) in the heart. The slow response to membrane depolarization is a hallmark feature of this channel's ...K7.1 is a cardiac voltage-gated potassium channel that underlies the delayed rectifier current (I) in the heart. The slow response to membrane depolarization is a hallmark feature of this channel's physiology, yet the mechanistic basis of how voltage promotes the open potassium conducting state is unknown. We focused on previously identified aromatic residues which might couple the pore and voltage-sensing domains (VSDs) by using a chemical tuning approach whereby aromatic residues are modified by serial fluorination. The data show that serial fluorination at one site (F232 on the S4 helix, within the VSD) resulted in a stepwise voltage-gating shift, where each added fluorine atom further biased channel opening to more negative voltages. Mutant-cycle analysis of proximal positively charged amino acids indicates that F232 likely forms a cation-π interaction with K285, a residue at the tip of the S5 segment in the pore domain. Using cryoelectron microscopy, a partial structure of the F232 penta-F-Phe K7.1 (KCNQ1) open channel was resolved to 6 Å. The data support a gating mechanism whereby the F232-K285 cation-π interaction represents an intermediate activated state that is broken prior to channel opening.
History
DepositionAug 21, 2025-
Header (metadata) releaseJan 21, 2026-
Map releaseJan 21, 2026-
UpdateFeb 4, 2026-
Current statusFeb 4, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_72248.png

Downloads & links

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Map

FileDownload / File: emd_72248.map.gz / Format: CCP4 / Size: 40.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationKCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and calmodulin
Projections & slices

Image control

Size
Brightness
Contrast
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AxesZ (Sec.)Y (Row.)X (Col.)
1.23 Å/pix.
x 220 pix.
= 269.72 Å		1.23 Å/pix.
x 220 pix.
= 269.72 Å		1.23 Å/pix.
x 220 pix.
= 269.72 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.226 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.7593835 - 0.7790945
Average (Standard dev.)0.004515577 (±0.027868949)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions220220220
Spacing220220220
CellA=B=C: 269.72 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Half Map A

Fileemd_72248_half_map_1.map
AnnotationHalf Map A
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half Map B

Fileemd_72248_half_map_2.map
AnnotationHalf Map B
Projections & Slices
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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : KCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and ca...

EntireName: KCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and calmodulin
Components
  • Complex: KCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and calmodulin

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Supramolecule #1: KCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and ca...

SupramoleculeName: KCNQ1 with F232 Penta-F-Phe mutation, complexed with KCNE1 and calmodulin
type: complex / ID: 1 / Parent: 0
Details: Recombinant human KCNQ1 cardiac potassium channel expressed with a pentafluoro-L-phenylalanine substitution for phenylalanine in the F232 site. Co-expressed and co-purified with KCNE1 and recombinant calmodulin.
Source (natural)Organism: Homo sapiens (human)

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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

Concentration3.5 mg/mL
BufferpH: 7.4
Component:
ConcentrationFormulaName
150.0 mMKClpotassium chloride
40.0 mMHEPES4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid
0.5 mMCaCl2calcium chloride
0.05 % w/vDigitonindigitonin
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
DetailsRecombinant human KCNQ1 cardiac potassium channel with a pentafluoro-L-phenylalanine substitution for phenylalanine in the F232 site, expressed in Hek293S GnTi- suspension cells. Co-expressed and co-purified with KCNE1 and recombinant calmodulin. The sample was purified over

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average exposure time: 0.15875 sec. / Average electron dose: 1.25 e/Å2
Details: 1.25 dose per frame, 50 e/A^2 total dose, 0.015875 sec/frame, 6.35 exposure time
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 6.43 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.7.1) / Number images used: 176031
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: NOT APPLICABLE

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