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- EMDB-61053: cryo-EM structure of human cystic fibrosis transmembrane conducta... -

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Basic information

Entry
Database: EMDB / ID: EMD-61053
Titlecryo-EM structure of human cystic fibrosis transmembrane conductance regulator (CFTR) from Biortus
Map datasharpened by deepEMhancer
Sample
  • Complex: human cystic fibrosis transmembrane conductance regulator (CFTR)
Keywordshuman cystic fibrosis transmembrane conductance regulator / CFTR / MEMBRANE PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsCao S / Shi H / Yang YH / Li JX / Hu YF
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Cell / Year: 2017
Title: Molecular Structure of the Human CFTR Ion Channel.
Authors: Fangyu Liu / Zhe Zhang / László Csanády / David C Gadsby / Jue Chen /
Abstract: The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of ...The cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette (ABC) transporter that uniquely functions as an ion channel. Here, we present a 3.9 Å structure of dephosphorylated human CFTR without nucleotides, determined by electron cryomicroscopy (cryo-EM). Close resemblance of this human CFTR structure to zebrafish CFTR under identical conditions reinforces its relevance for understanding CFTR function. The human CFTR structure reveals a previously unresolved helix belonging to the R domain docked inside the intracellular vestibule, precluding channel opening. By analyzing the sigmoid time course of CFTR current activation, we propose that PKA phosphorylation of the R domain is enabled by its infrequent spontaneous disengagement, which also explains residual ATPase and gating activity of dephosphorylated CFTR. From comparison with MRP1, a feature distinguishing CFTR from all other ABC transporters is the helix-loop transition in transmembrane helix 8, which likely forms the structural basis for CFTR's channel function.
History
DepositionAug 2, 2024-
Header (metadata) releaseSep 4, 2024-
Map releaseSep 4, 2024-
UpdateSep 4, 2024-
Current statusSep 4, 2024Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_61053.png

Downloads & links

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Map

FileDownload / File: emd_61053.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharpened by deepEMhancer
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.95 Å/pix.
x 288 pix.
= 273.6 Å		0.95 Å/pix.
x 288 pix.
= 273.6 Å		0.95 Å/pix.
x 288 pix.
= 273.6 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.95 Å
Density

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Histogram (log scale)
Contour LevelBy AUTHOR: 0.125
Minimum - Maximum-0.040876757 - 1.8807614
Average (Standard dev.)0.0007733769 (±0.017707909)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 273.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_61053_msk_1.map
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Additional map: unsharpened map

Fileemd_61053_additional_1.map
Annotationunsharpened map
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Additional map: sharpened by cryoSPARC

Fileemd_61053_additional_2.map
Annotationsharpened by cryoSPARC
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Half map: halfmap B

Fileemd_61053_half_map_1.map
Annotationhalfmap B
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Half map: halfmap A

Fileemd_61053_half_map_2.map
Annotationhalfmap A
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Sample components

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Entire : human cystic fibrosis transmembrane conductance regulator (CFTR)

EntireName: human cystic fibrosis transmembrane conductance regulator (CFTR)
Components
  • Complex: human cystic fibrosis transmembrane conductance regulator (CFTR)

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Supramolecule #1: human cystic fibrosis transmembrane conductance regulator (CFTR)

SupramoleculeName: human cystic fibrosis transmembrane conductance regulator (CFTR)
type: complex / ID: 1 / Parent: 0
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

Concentration8.15 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 55.0 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: EMDB MAP
EMDB ID:

8516

Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 375610
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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