+Open data
-Basic information
Entry | Database: PDB / ID: 7cu3 | ||||||||||||||||||
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Title | Structure of mammalian NALCN-FAM155A complex at 2.65 angstrom | ||||||||||||||||||
Components |
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Keywords | TRANSPORT PROTEIN / NALCN / Channel / FAM155 / NCA / NLF | ||||||||||||||||||
Function / homology | Function and homology information Stimuli-sensing channels / positive regulation of synaptic transmission, cholinergic / leak channel activity / regulation of resting membrane potential / voltage-gated sodium channel activity / monoatomic ion channel complex / calcium ion import across plasma membrane / sodium ion transmembrane transport / monoatomic cation channel activity / potassium ion transmembrane transport ...Stimuli-sensing channels / positive regulation of synaptic transmission, cholinergic / leak channel activity / regulation of resting membrane potential / voltage-gated sodium channel activity / monoatomic ion channel complex / calcium ion import across plasma membrane / sodium ion transmembrane transport / monoatomic cation channel activity / potassium ion transmembrane transport / positive regulation of synaptic transmission, GABAergic / calcium ion transmembrane transport / plasma membrane Similarity search - Function | ||||||||||||||||||
Biological species | Rattus norvegicus (Norway rat) Mus musculus (house mouse) | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.65 Å | ||||||||||||||||||
Authors | Chen, L. / Kang, Y. | ||||||||||||||||||
Funding support | China, 5items
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Citation | Journal: Nat Commun / Year: 2020 Title: Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex. Authors: Yunlu Kang / Jing-Xiang Wu / Lei Chen / Abstract: Resting membrane potential determines the excitability of the cell and is essential for the cellular electrical activities. The NALCN channel mediates sodium leak currents, which positively adjust ...Resting membrane potential determines the excitability of the cell and is essential for the cellular electrical activities. The NALCN channel mediates sodium leak currents, which positively adjust resting membrane potential towards depolarization. The NALCN channel is involved in several neurological processes and has been implicated in a spectrum of neurodevelopmental diseases. Here, we report the cryo-EM structure of rat NALCN and mouse FAM155A complex to 2.7 Å resolution. The structure reveals detailed interactions between NALCN and the extracellular cysteine-rich domain of FAM155A. We find that the non-canonical architecture of NALCN selectivity filter dictates its sodium selectivity and calcium block, and that the asymmetric arrangement of two functional voltage sensors confers the modulation by membrane potential. Moreover, mutations associated with human diseases map to the domain-domain interfaces or the pore domain of NALCN, intuitively suggesting their pathological mechanisms. | ||||||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7cu3.cif.gz | 290.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7cu3.ent.gz | 230.7 KB | Display | PDB format |
PDBx/mmJSON format | 7cu3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7cu3_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 7cu3_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 7cu3_validation.xml.gz | 53.2 KB | Display | |
Data in CIF | 7cu3_validation.cif.gz | 78.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cu/7cu3 ftp://data.pdbj.org/pub/pdb/validation_reports/cu/7cu3 | HTTPS FTP |
-Related structure data
Related structure data | 30470MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 200682.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Nalcn, Nca, Rb21, Vgcnl1 / Production host: Homo sapiens (human) / References: UniProt: Q6Q760 | ||||||
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#2: Protein | Mass: 52795.801 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Fam155a / Production host: Homo sapiens (human) / References: UniProt: Q8CCS2 | ||||||
#3: Sugar | #4: Chemical | ChemComp-6OU / [( #5: Chemical | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: NALCN-FAM155A complex / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Homo sapiens (human) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.18rc1_3777: / Classification: refinement | ||||||||||||||||||||||||
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EM software | Name: cisTEM / Category: 3D reconstruction | ||||||||||||||||||||||||
CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.65 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 135043 / Symmetry type: POINT | ||||||||||||||||||||||||
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