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Open data
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Basic information
Entry | Database: PDB / ID: 6bqn | ||||||
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Title | Cryo-EM structure of ENaC | ||||||
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![]() | MEMBRANE PROTEIN / sodium channel | ||||||
Function / homology | ![]() : / : / sensory perception of salty taste / Sensory perception of salty taste / aldosterone metabolic process / neutrophil-mediated killing of bacterium / sensory perception of sour taste / leukocyte activation involved in inflammatory response / cellular response to vasopressin / sperm principal piece ...: / : / sensory perception of salty taste / Sensory perception of salty taste / aldosterone metabolic process / neutrophil-mediated killing of bacterium / sensory perception of sour taste / leukocyte activation involved in inflammatory response / cellular response to vasopressin / sperm principal piece / sodium channel complex / ligand-gated sodium channel activity / epithelial fluid transport / sodium ion homeostasis / artery smooth muscle contraction / mucus secretion / WW domain binding / neutrophil activation involved in immune response / cellular response to aldosterone / multicellular organismal-level water homeostasis / cellular response to acidic pH / sodium ion import across plasma membrane / potassium ion homeostasis / intracellular sodium ion homeostasis / motile cilium / erythrocyte homeostasis / sodium channel activity / response to food / ciliary membrane / sodium ion transport / sodium ion transmembrane transport / acrosomal vesicle / regulation of blood pressure / cytoplasmic vesicle membrane / multicellular organism growth / Stimuli-sensing channels / monoatomic ion channel activity / gene expression / apical plasma membrane / response to xenobiotic stimulus / external side of plasma membrane / extracellular exosome / nucleoplasm / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||
![]() | Noreng, S. / Bharadwaj, A. / Posert, R. / Yoshioka, C. / Baconguis, I. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the human epithelial sodium channel by cryo-electron microscopy. Authors: Sigrid Noreng / Arpita Bharadwaj / Richard Posert / Craig Yoshioka / Isabelle Baconguis / ![]() Abstract: The epithelial sodium channel (ENaC), a member of the ENaC/DEG superfamily, regulates Na and water homeostasis. ENaCs assemble as heterotrimeric channels that harbor protease-sensitive domains ...The epithelial sodium channel (ENaC), a member of the ENaC/DEG superfamily, regulates Na and water homeostasis. ENaCs assemble as heterotrimeric channels that harbor protease-sensitive domains critical for gating the channel. Here, we present the structure of human ENaC in the uncleaved state determined by single-particle cryo-electron microscopy. The ion channel is composed of a large extracellular domain and a narrow transmembrane domain. The structure reveals that ENaC assembles with a 1:1:1 stoichiometry of α:β:γ subunits arranged in a counter-clockwise manner. The shape of each subunit is reminiscent of a hand with key gating domains of a 'finger' and a 'thumb.' Wedged between these domains is the elusive protease-sensitive inhibitory domain poised to regulate conformational changes of the 'finger' and 'thumb'; thus, the structure provides the first view of the architecture of inhibition of ENaC. | ||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 290.2 KB | Display | ![]() |
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PDB format | ![]() | 236.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 7130MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Antibody , 7 types, 7 molecules ABCDEFG
#1: Antibody | Mass: 54038.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to ...Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to flexible areas of the protein where density is missing. The full sequence is described in sequence details. Source: (gene. exp.) ![]() ![]() |
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#2: Antibody | Mass: 55038.633 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to ...Details: Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to flexible areas of the protein where density is missing. The full sequence is described in sequence details. Source: (gene. exp.) ![]() ![]() |
#3: Antibody | Mass: 55834.457 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The protein is EGFP-SCNN1G chimera. Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. ...Details: The protein is EGFP-SCNN1G chimera. Transmembrane helices have been built with poly UNK since the density for the transmembrane domain is not good enough to accurately build a model. Residues that have not been built is due to flexible areas of the protein where density is missing. The first 260 residues is a His8 tag and a strep-tag followed by EGFP (UniProt accession code: C5MKY7). The full sequence is described in sequence details. Source: (gene. exp.) ![]() ![]() |
#4: Antibody | Mass: 9039.134 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Sequence unknown, built with poly UNK. / Source: (natural) ![]() ![]() |
#5: Antibody | Mass: 10315.707 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Sequence unknown, built with poly UNK. / Source: (natural) ![]() ![]() |
#6: Antibody | Mass: 9805.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Sequence unknown, built with poly UNK. / Source: (natural) ![]() ![]() |
#7: Antibody | Mass: 9549.763 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Sequence unknown, built with poly UNK. / Source: (natural) ![]() ![]() |
-Details
Sequence details | The sequence of SCNNIA is MAEEEALIEFHRSYRELFEFFANNTTIHGAIRLVSSQHNRMKTAFWAVLWLATFGMMYWQFGLLFGEY ...The sequence of SCNNIA is MAEEEALIEF |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Membrane protein complex / Type: CELL / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: OTHER |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.13_2998: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 304615 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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