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- PDB-5uak: Dephosphorylated, ATP-free human cystic fibrosis transmembrane co... -

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Basic information

Entry
Database: PDB / ID: 5uak
TitleDephosphorylated, ATP-free human cystic fibrosis transmembrane conductance regulator (CFTR)
Components(Cystic fibrosis transmembrane conductance regulator) x 2
KeywordsMEMBRANE PROTEIN / HYDROLASE / ABC transporter / anion channel / cystic fibrosis / membrane protein / hydrolase
Function / homologyCystic fibrosis TM conductance regulator (CFTR), regulator domain / ABC transporter-like / ABC transporter type 1, transmembrane domain / ABC transporter, conserved site / CFTR regulator domain / P-loop containing nucleoside triphosphate hydrolase / ABC transporter type 1, transmembrane domain superfamily / ABC transporter / ABC transporter transmembrane region / ABC transporters family signature. ...Cystic fibrosis TM conductance regulator (CFTR), regulator domain / ABC transporter-like / ABC transporter type 1, transmembrane domain / ABC transporter, conserved site / CFTR regulator domain / P-loop containing nucleoside triphosphate hydrolase / ABC transporter type 1, transmembrane domain superfamily / ABC transporter / ABC transporter transmembrane region / ABC transporters family signature. / AAA+ ATPase domain / ATP-binding cassette, ABC transporter-type domain profile. / ABC transporter integral membrane type-1 fused domain profile. / ABC-family proteins mediated transport / RHO GTPases regulate CFTR trafficking / Defective CFTR causes cystic fibrosis / Ub-specific processing proteases / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / Cystic fibrosis transmembrane conductance regulator / ATPase-coupled anion transmembrane transporter activity / positive regulation of cyclic nucleotide-gated ion channel activity / positive regulation of voltage-gated chloride channel activity / channel-conductance-controlling ATPase / intracellularly ATP-gated chloride channel activity / transepithelial water transport / intracellular pH elevation / bicarbonate transmembrane transporter activity / Golgi-associated vesicle membrane / multicellular organismal water homeostasis / chloride transmembrane transporter activity / chloride channel regulator activity / chloride channel inhibitor activity / chloride channel activity / vesicle docking involved in exocytosis / chloride channel complex / chloride transmembrane transport / cholesterol transport / membrane hyperpolarization / positive regulation of exocytosis / cellular response to forskolin / ATPase activity, coupled to transmembrane movement of substances / positive regulation of insulin secretion involved in cellular response to glucose stimulus / sperm capacitation / cholesterol biosynthetic process / recycling endosome / clathrin-coated vesicle membrane / PDZ domain binding / cellular response to cAMP / recycling endosome membrane / transmembrane transport / lysosomal membrane / bicarbonate transport / membrane organization / early endosome membrane / apical plasma membrane / ATPase activity / early endosome / endosome membrane / protein deubiquitination / endoplasmic reticulum membrane / integral component of plasma membrane / cell surface / enzyme binding / protein-containing complex / integral component of membrane / extracellular exosome / ATP binding / plasma membrane / nucleus / cytosol / cytoplasm / Cystic fibrosis transmembrane conductance regulator
Function and homology information
Specimen sourceHomo sapiens / / human
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 3.87 Å resolution
AuthorsLiu, F. / Zhang, Z. / Chen, J.
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.
Copyright: 2017 Elsevier Inc. All rights reserved.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Dec 19, 2016 / Release: Jan 18, 2017
RevisionDateData content typeGroupProviderType
1.0Jan 18, 2017Structure modelrepositoryInitial release
1.1Mar 1, 2017Structure modelOther
1.2Mar 29, 2017Structure modelDatabase references
1.3Apr 12, 2017Structure modelDatabase references

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Assembly

Deposited unit
A: Cystic fibrosis transmembrane conductance regulator
R: Cystic fibrosis transmembrane conductance regulator


Theoretical massNumber of molelcules
Total (without water)170,9892
Polyers170,9892
Non-polymers00
Water0
1


TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein/peptide Cystic fibrosis transmembrane conductance regulator / / CFTR / ATP-binding cassette sub-family C member 7 / Channel conductance-controlling ATPase / cAMP-dependent chloride channel


Mass: 169353.578 Da / Num. of mol.: 1 / Source: (gene. exp.) Homo sapiens / / human
Gene: CFTR, ABCC7Cystic fibrosis transmembrane conductance regulator
Cell line (production host): HEK293S GnTI- / Production host: Homo sapiens
References: UniProt:P13569, EC:3.6.3.49 (channel-conductance-controlling ATPase)
#2: Protein/peptide Cystic fibrosis transmembrane conductance regulator / / CFTR / ATP-binding cassette sub-family C member 7 / Channel conductance-controlling ATPase / cAMP-dependent chloride channel


Mass: 1635.006 Da / Num. of mol.: 1 / Fragment: R domain / Source: (gene. exp.) Homo sapiens / / human
Gene: CFTR, ABCC7Cystic fibrosis transmembrane conductance regulator
Cell line (production host): HEK293S GnTI- / Production host: Homo sapiens

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: human cystic fibrosis transmembrane conductance regulator (CFTR)
Type: COMPLEX / Entity ID: 1, 2 / Source: RECOMBINANT
Molecular weightValue: 168 deg. / Units: KILODALTONS/NANOMETER / Experimental value: NO
Source (natural)Organism: Homo sapiens
Source (recombinant)Cell: HEK293S GnTI- / Organism: Homo sapiens / Plasmid: BacMam
Buffer solutionpH: 7.5
SpecimenConc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK I / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 298 kelvins

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyMicroscope model: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 1.68 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 3.87 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 415915 / Symmetry type: POINT

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