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- PDB-6uzz: structure of human KCNQ1-CaM complex -

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Basic information

Entry
Database: PDB / ID: 6uzz
Titlestructure of human KCNQ1-CaM complex
Components
  • Calmodulin-1
  • Potassium voltage-gated channel subfamily KQT member 1
KeywordsMEMBRANE PROTEIN / potassium channel / KCNQ1 / CaM
Function / homology
Function and homology information


negative regulation of voltage-gated potassium channel activity / voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization / regulation of gastric acid secretion / regulation of atrial cardiac muscle cell membrane repolarization / membrane repolarization during atrial cardiac muscle cell action potential / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization / membrane repolarization during ventricular cardiac muscle cell action potential / membrane repolarization during action potential / membrane repolarization during cardiac muscle cell action potential ...negative regulation of voltage-gated potassium channel activity / voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization / regulation of gastric acid secretion / regulation of atrial cardiac muscle cell membrane repolarization / membrane repolarization during atrial cardiac muscle cell action potential / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization / membrane repolarization during ventricular cardiac muscle cell action potential / membrane repolarization during action potential / membrane repolarization during cardiac muscle cell action potential / atrial cardiac muscle cell action potential / potassium ion export across plasma membrane / regulation of membrane repolarization / ion channel complex / outward rectifier potassium channel activity / negative regulation of delayed rectifier potassium channel activity / regulation of ventricular cardiac muscle cell membrane repolarization / positive regulation of potassium ion transmembrane transport / gene silencing / delayed rectifier potassium channel activity / positive regulation of cardiac muscle contraction / ventricular cardiac muscle cell action potential / cardiac conduction / positive regulation of heart rate / protein phosphatase 1 binding / circulatory system development => GO:0072359 / regulation of heart rate by cardiac conduction / regulation of gene expression by genetic imprinting / intestinal absorption / glycogen catabolic process / establishment of protein localization to mitochondrial membrane / N-terminal myristoylation domain binding / type 3 metabotropic glutamate receptor binding / regulation of cell communication by electrical coupling involved in cardiac conduction / negative regulation of peptidyl-threonine phosphorylation / regulation of high voltage-gated calcium channel activity / regulation of synaptic vesicle endocytosis / protein phosphatase activator activity / positive regulation of ryanodine-sensitive calcium-release channel activity / potassium ion transmembrane transport / regulation of rhodopsin mediated signaling pathway / renal absorption / detection of calcium ion / catalytic complex / protein kinase A regulatory subunit binding / response to corticosterone / adenylate cyclase binding / positive regulation of cyclic-nucleotide phosphodiesterase activity / inositol phosphate metabolic process / adenylate cyclase activator activity / inner ear development / voltage-gated potassium channel activity / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / cardiac muscle contraction / regulation of heart contraction / activation of adenylate cyclase activity / calcium channel inhibitor activity / Wnt signaling pathway, calcium modulating pathway / positive regulation of phosphoprotein phosphatase activity / nitric-oxide synthase binding / protein kinase A catalytic subunit binding / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / voltage-gated potassium channel complex / titin binding / substantia nigra development / calcium channel complex / sarcomere / cellular response to epinephrine stimulus / positive regulation of protein dephosphorylation / phosphatidylinositol 3-kinase binding / regulation of heart rate / regulation of ryanodine-sensitive calcium-release channel activity / protein serine/threonine kinase activator activity / positive regulation of protein autophosphorylation / mitochondrial membrane / enzyme regulator activity / response to amphetamine / positive regulation of peptidyl-threonine phosphorylation / positive regulation of protein serine/threonine kinase activity / cellular response to cAMP / regulation of cytokinesis / regulation of nitric-oxide synthase activity / nitric-oxide synthase regulator activity / phosphatidylinositol-4,5-bisphosphate binding / regulation of synaptic vesicle exocytosis / positive regulation of DNA binding / spindle microtubule / sensory perception of sound / calcium-mediated signaling / synaptic vesicle membrane / muscle contraction / microtubule cytoskeleton organization / response to calcium ion / spindle pole / positive regulation of nitric-oxide synthase activity / calcium-dependent protein binding / cellular response to drug / platelet degranulation
EF-hand domain pair / Ion transport domain / KCNQ voltage-gated potassium channel / Ion transport protein / Calmodulin / Voltage-gated potassium channel / EF-Hand 1, calcium-binding site / EF-hand domain / Potassium channel, voltage dependent, KCNQ, C-terminal / Potassium channel, voltage dependent, KCNQ ...EF-hand domain pair / Ion transport domain / KCNQ voltage-gated potassium channel / Ion transport protein / Calmodulin / Voltage-gated potassium channel / EF-Hand 1, calcium-binding site / EF-hand domain / Potassium channel, voltage dependent, KCNQ, C-terminal / Potassium channel, voltage dependent, KCNQ / EF-hand domain pair / Potassium channel, voltage dependent, KCNQ1
Calmodulin-1 / Potassium voltage-gated channel subfamily KQT member 1
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsMackinnon, R. / Sun, J.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)5K99HL143037 United States
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Cell / Year: 2020
Title: Structural Basis of Human KCNQ1 Modulation and Gating.
Authors: Ji Sun / Roderick MacKinnon /
Abstract: KCNQ1, also known as Kv7.1, is a voltage-dependent K channel that regulates gastric acid secretion, salt and glucose homeostasis, and heart rhythm. Its functional properties are regulated in a tissue- ...KCNQ1, also known as Kv7.1, is a voltage-dependent K channel that regulates gastric acid secretion, salt and glucose homeostasis, and heart rhythm. Its functional properties are regulated in a tissue-specific manner through co-assembly with beta subunits KCNE1-5. In non-excitable cells, KCNQ1 forms a complex with KCNE3, which suppresses channel closure at negative membrane voltages that otherwise would close it. Pore opening is regulated by the signaling lipid PIP2. Using cryoelectron microscopy (cryo-EM), we show that KCNE3 tucks its single-membrane-spanning helix against KCNQ1, at a location that appears to lock the voltage sensor in its depolarized conformation. Without PIP2, the pore remains closed. Upon addition, PIP2 occupies a site on KCNQ1 within the inner membrane leaflet, which triggers a large conformational change that leads to dilation of the pore's gate. It is likely that this mechanism of PIP2 activation is conserved among Kv7 channels.
Validation Report
SummaryFull reportAbout validation report
History
DepositionNov 16, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 4, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Jan 15, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.3Feb 5, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year

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Structure visualization

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Assembly

Deposited unit
A: Potassium voltage-gated channel subfamily KQT member 1
B: Calmodulin-1
C: Potassium voltage-gated channel subfamily KQT member 1
D: Calmodulin-1
E: Potassium voltage-gated channel subfamily KQT member 1
F: Calmodulin-1
G: Potassium voltage-gated channel subfamily KQT member 1
H: Calmodulin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)320,76516
Polymers320,4448
Non-polymers3218
Water0
1


TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein
Potassium voltage-gated channel subfamily KQT member 1 / IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 / KQT-like 1 / Voltage- ...IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 / KQT-like 1 / Voltage-gated potassium channel subunit Kv7.1


Mass: 63258.574 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KCNQ1, KCNA8, KCNA9, KVLQT1 / Production host: Homo sapiens (human) / References: UniProt: P51787
#2: Protein
Calmodulin-1 /


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
#3: Chemical
ChemComp-CA / CALCIUM ION / Calcium


Mass: 40.078 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Ca
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: KCNQ1-CaM complex / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: 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: 94 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.13_2998: / Classification: refinement
EM softwareName: RELION / Category: 3D reconstruction
CTF correctionType: NONE
SymmetryPoint symmetry: C4 (4 fold cyclic)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 66746 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL

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