|Entry||Database: PDB / ID: 6pbx|
|Title||Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 3-13 deletion mutant bound to calmodulin (conformation 2)|
|Keywords||TRANSPORT PROTEIN/CALCIUM BINDING PROTEIN / Voltage-gated potassium channel / ion channel / calmodulin / TRANSPORT PROTEIN-CALCIUM BINDING PROTEIN complex|
|Function / homology|
Function and homology information
voltage-gated ion channel activity involved in regulation of presynaptic membrane potential / regulation of presynaptic cytosolic calcium ion concentration / potassium channel complex / delayed rectifier potassium channel activity / phosphatidylinositol bisphosphate binding / parallel fiber to Purkinje cell synapse / nuclear inner membrane / startle response / axolemma / 14-3-3 protein binding ...voltage-gated ion channel activity involved in regulation of presynaptic membrane potential / regulation of presynaptic cytosolic calcium ion concentration / potassium channel complex / delayed rectifier potassium channel activity / phosphatidylinositol bisphosphate binding / parallel fiber to Purkinje cell synapse / nuclear inner membrane / startle response / axolemma / 14-3-3 protein binding / glycogen catabolic process / N-terminal myristoylation domain binding / regulation of cell communication by electrical coupling involved in cardiac conduction / inositol phosphate metabolic process / negative regulation of peptidyl-threonine phosphorylation / protein phosphatase activator activity / positive regulation of ryanodine-sensitive calcium-release channel activity / potassium ion transmembrane transport / regulation of rhodopsin mediated signaling pathway / detection of calcium ion / catalytic complex / voltage-gated potassium channel complex / adenylate cyclase binding / positive regulation of cyclic-nucleotide phosphodiesterase activity / adenylate cyclase activator activity / voltage-gated potassium channel activity / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction / regulation of ion transmembrane transport / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / calcium channel inhibitor activity / positive regulation of phosphoprotein phosphatase activity / Wnt signaling pathway, calcium modulating pathway / positive regulation of protein dephosphorylation / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / go:0051186: / titin binding / substantia nigra development / calcium channel complex / sarcomere / regulation of ryanodine-sensitive calcium-release channel activity / regulation of heart rate / protein serine/threonine kinase activator activity / positive regulation of protein autophosphorylation / cellular response to calcium ion / enzyme regulator activity / postsynaptic density membrane / phosphatidylinositol-mediated signaling / ion transmembrane transport / regulation of synaptic vesicle exocytosis / spindle microtubule / regulation of membrane potential / positive regulation of peptidyl-threonine phosphorylation / integral component of presynaptic membrane / positive regulation of protein serine/threonine kinase activity / regulation of nitric-oxide synthase activity / regulation of cytokinesis / presynaptic membrane / calcium-mediated signaling / muscle contraction / response to calcium ion / microtubule cytoskeleton organization / spindle pole / platelet degranulation / Fc-epsilon receptor signaling pathway / early endosome membrane / disordered domain specific binding / regulation of cell population proliferation / ion channel binding / perikaryon / vesicle / calmodulin binding / MAPK cascade / centrosome / G protein-coupled receptor signaling pathway / synapse / axon / protein domain specific binding / neuronal cell body / dendrite / protein-containing complex binding / calcium ion binding / protein kinase binding / viral process / perinuclear region of cytoplasm / cell surface / integral component of plasma membrane / protein-containing complex / extracellular region / nucleoplasm / identical protein binding / plasma membrane / nucleus / cytosol / cytoplasm
EF-hand domain pair / Potassium voltage-gated channel subfamily H member 1 / PAS domain / Cyclic nucleotide-binding domain / PAS-associated, C-terminal / EF-hand domain / Potassium channel, voltage-dependent, EAG/ELK/ERG / Potassium channel, voltage-dependent, EAG / Ion transport domain / EF-hand domain pair ...EF-hand domain pair / Potassium voltage-gated channel subfamily H member 1 / PAS domain / Cyclic nucleotide-binding domain / PAS-associated, C-terminal / EF-hand domain / Potassium channel, voltage-dependent, EAG/ELK/ERG / Potassium channel, voltage-dependent, EAG / Ion transport domain / EF-hand domain pair / RmlC-like jelly roll fold / EF-Hand 1, calcium-binding site / Cyclic nucleotide-binding-like / Voltage-dependent channel domain superfamily / PAC motif / PAS domain superfamily / Calmodulin / Cyclic nucleotide-binding domain / Ion transport protein / PAS domain
Calmodulin-1 / Potassium voltage-gated channel subfamily H member 1
|Biological species||Rattus norvegicus (Norway rat)|
Homo sapiens (human)
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å|
|Authors||Whicher, J.R. / MacKinnon, R.|
|Funding support|| United States, 3items |
|Citation||Journal: Elife / Year: 2019|
Title: Regulation of Eag1 gating by its intracellular domains.
Authors: Jonathan R Whicher / Roderick MacKinnon /
Abstract: Voltage-gated potassium channels (Ks) are gated by transmembrane voltage sensors (VS) that move in response to changes in membrane voltage. K10.1 or Eag1 also has three intracellular domains: PAS, C- ...Voltage-gated potassium channels (Ks) are gated by transmembrane voltage sensors (VS) that move in response to changes in membrane voltage. K10.1 or Eag1 also has three intracellular domains: PAS, C-linker, and CNBHD. We demonstrate that the Eag1 intracellular domains are not required for voltage-dependent gating but likely interact with the VS to modulate gating. We identified specific interactions between the PAS, CNBHD, and VS that modulate voltage-dependent gating and provide evidence that VS movement destabilizes these interactions to promote channel opening. Additionally, mutation of these interactions renders Eag1 insensitive to calmodulin inhibition. The structure of the calmodulin insensitive mutant in a pre-open conformation suggests that channel opening may occur through a rotation of the intracellular domains and calmodulin may prevent this rotation by stabilizing interactions between the VS and intracellular domains. Intracellular domains likely play a similar modulatory role in voltage-dependent gating of the related K11-12 channels.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: Potassium voltage-gated channel subfamily H member 1
C: Potassium voltage-gated channel subfamily H member 1
E: Potassium voltage-gated channel subfamily H member 1
G: Potassium voltage-gated channel subfamily H member 1
Mass: 96261.430 Da / Num. of mol.: 4 / Fragment: UNP residues 14-773,888-962
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Kcnh1, Eag / Production host: Homo sapiens (human) / References: UniProt: Q63472
Mass: 16852.545 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CALM1, CALM, CAM, CAM1 / Production host: Homo sapiens (human) / References: UniProt: P0DP23
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Buffer solution||pH: 8|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Details: unspecified|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
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|
|Image recording||Electron dose: 1.6 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)|
|Software||Name: PHENIX / Version: 1.14_3260: / Classification: refinement|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C4 (4 fold cyclic)|
|3D reconstruction||Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 54530 / Symmetry type: POINT|
|Atomic model building||Protocol: FLEXIBLE FIT / Space: REAL|
|Atomic model building||PDB-ID: 5K7L|
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