+Open data
-Basic information
Entry | Database: PDB / ID: 6v22 | ||||||
---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of Ca2+-bound hsSlo1-beta4 channel complex | ||||||
Components | (Calcium-activated potassium channel subunit ...) x 2 | ||||||
Keywords | TRANSPORT PROTEIN / High conductance Ca2+-activated K+ channel / Slo1 channel / BK channel / MaxiK channel / Slo1 beta subunit / beta4 subunit | ||||||
Function / homology | Function and homology information Acetylcholine inhibits contraction of outer hair cells / large conductance calcium-activated potassium channel activity / micturition / Ca2+ activated K+ channels / response to carbon monoxide / calcium-activated potassium channel activity / negative regulation of cell volume / regulation of neurotransmitter secretion / smooth muscle contraction involved in micturition / intracellular potassium ion homeostasis ...Acetylcholine inhibits contraction of outer hair cells / large conductance calcium-activated potassium channel activity / micturition / Ca2+ activated K+ channels / response to carbon monoxide / calcium-activated potassium channel activity / negative regulation of cell volume / regulation of neurotransmitter secretion / smooth muscle contraction involved in micturition / intracellular potassium ion homeostasis / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / Sensory processing of sound by inner hair cells of the cochlea / response to osmotic stress / action potential / cGMP effects / voltage-gated potassium channel activity / neuronal action potential / regulation of vasoconstriction / detection of calcium ion / potassium channel regulator activity / voltage-gated potassium channel complex / potassium ion transmembrane transport / regulation of membrane potential / caveola / potassium ion transport / vasodilation / response to calcium ion / actin binding / chemical synaptic transmission / postsynaptic membrane / response to hypoxia / positive regulation of apoptotic process / apical plasma membrane / synapse / membrane / identical protein binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||
Authors | Tao, X. / MacKinnon, R. | ||||||
Funding support | United States, 1items
| ||||||
Citation | Journal: Elife / Year: 2019 Title: Molecular structures of the human Slo1 K channel in complex with β4. Authors: Xiao Tao / Roderick MacKinnon / Abstract: Slo1 is a Ca- and voltage-activated K channel that underlies skeletal and smooth muscle contraction, audition, hormone secretion and neurotransmitter release. In mammals, Slo1 is regulated by ...Slo1 is a Ca- and voltage-activated K channel that underlies skeletal and smooth muscle contraction, audition, hormone secretion and neurotransmitter release. In mammals, Slo1 is regulated by auxiliary proteins that confer tissue-specific gating and pharmacological properties. This study presents cryo-EM structures of Slo1 in complex with the auxiliary protein, β4. Four β4, each containing two transmembrane helices, encircle Slo1, contacting it through helical interactions inside the membrane. On the extracellular side, β4 forms a tetrameric crown over the pore. Structures with high and low Ca concentrations show that identical gating conformations occur in the absence and presence of β4, implying that β4 serves to modulate the relative stabilities of 'pre-existing' conformations rather than creating new ones. The effects of β4 on scorpion toxin inhibition kinetics are explained by the crown, which constrains access but does not prevent binding. | ||||||
History |
|
-Structure visualization
Movie |
Movie viewer |
---|---|
Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6v22.cif.gz | 823.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6v22.ent.gz | 688.7 KB | Display | PDB format |
PDBx/mmJSON format | 6v22.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v2/6v22 ftp://data.pdbj.org/pub/pdb/validation_reports/v2/6v22 | HTTPS FTP |
---|
-Related structure data
Related structure data | 21025MC 6v35C 6v38C 6v3gC M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
-Calcium-activated potassium channel subunit ... , 2 types, 8 molecules ABCDEFGH
#1: Protein | Mass: 119988.062 Da / Num. of mol.: 4 / Fragment: UNP residues 66-1121 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCNMA1, KCNMA, SLO / Cell line (production host): HEK293S GnTI- / Production host: Homo sapiens (human) / References: UniProt: Q12791 #2: Protein | Mass: 24991.756 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KCNMB4 / Cell line (production host): HEK293S GnTI- / Production host: Homo sapiens (human) / References: UniProt: Q86W47 |
---|
-Sugars , 1 types, 8 molecules
#8: Sugar | ChemComp-NAG / |
---|
-Non-polymers , 5 types, 92 molecules
#3: Chemical | ChemComp-MG / #4: Chemical | ChemComp-CA / #5: Chemical | ChemComp-POV / ( #6: Chemical | ChemComp-CLR / #7: Chemical | ChemComp-K / |
---|
-Details
Has ligand of interest | Y |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: hsSlo1 alpha subunit-beta4 subunit complex / Type: COMPLEX Details: human high conductance Ca2+-activated K+ channel Slo1 (BK) alpha subunit and beta4 subunit Entity ID: #1-#2 / Source: RECOMBINANT | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Molecular weight | Value: 0.58 MDa / Experimental value: NO | ||||||||||||||||||||||||||||||
Source (natural) | Organism: Homo sapiens (human) | ||||||||||||||||||||||||||||||
Source (recombinant) | Organism: Homo sapiens (human) / Cell: HEK293S GnTI- | ||||||||||||||||||||||||||||||
Buffer solution | pH: 8 | ||||||||||||||||||||||||||||||
Buffer component |
| ||||||||||||||||||||||||||||||
Specimen | Conc.: 8.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 295 K / Details: Blot for 4 seconds before plunging. |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2000 nm / Nominal defocus min: 700 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 10 sec. / Electron dose: 74 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 5410 |
Image scans | Movie frames/image: 50 / Used frames/image: 1-50 |
-Processing
EM software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: NONE | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C4 (4 fold cyclic) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 117791 / Num. of class averages: 1 / Symmetry type: POINT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomic model building |
|