[English] 日本語
Yorodumi
- PDB-7mjq: Vascular KATP channel: Kir6.1 SUR2B quatrefoil-like conformation 2 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7mjq
TitleVascular KATP channel: Kir6.1 SUR2B quatrefoil-like conformation 2
Components
  • ATP-sensitive inward rectifier potassium channel 8
  • Isoform SUR2B of ATP-binding cassette sub-family C member 9
KeywordsTRANSPORT PROTEIN / KATP / potassium channel / vascular
Function / homology
Function and homology information


cardiac pacemaker cell differentiation / atrioventricular node cell differentiation / vascular process in circulatory system / substrate-dependent cell migration, cell contraction / oxygen metabolic process / reactive oxygen species biosynthetic process / reactive gliosis / response to decreased oxygen levels / ATP sensitive Potassium channels / response to peptide ...cardiac pacemaker cell differentiation / atrioventricular node cell differentiation / vascular process in circulatory system / substrate-dependent cell migration, cell contraction / oxygen metabolic process / reactive oxygen species biosynthetic process / reactive gliosis / response to decreased oxygen levels / ATP sensitive Potassium channels / response to peptide / ABC-family proteins mediated transport / response to resveratrol / ATP-activated inward rectifier potassium channel activity / membrane repolarization during ventricular cardiac muscle cell action potential / glutamate secretion, neurotransmission / inward rectifying potassium channel / sulfonylurea receptor activity / NLRP3 inflammasome complex assembly / ventricular cardiac muscle tissue development / response to hydrogen sulfide / voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization / response to potassium ion / cardiac conduction / CAMKK-AMPK signaling cascade / circulatory system development / response to oxygen levels / cellular response to potassium ion / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / coronary vasculature development / ATPase-coupled monoatomic cation transmembrane transporter activity / cellular response to chemical stress / vasculature development / regulation of monoatomic ion transmembrane transport / nervous system process / cardiac muscle cell contraction / synaptic assembly at neuromuscular junction / regulation of potassium ion transmembrane transport / inorganic cation transmembrane transport / blood circulation / syntaxin binding / sulfonylurea receptor binding / cellular respiration / response to stress / neuromuscular process / heterocyclic compound binding / cellular response to ATP / Ion homeostasis / establishment of cell polarity / response to ATP / myofibril / action potential / blood vessel development / response to exogenous dsRNA / fat cell differentiation / transmission of nerve impulse / potassium ion import across plasma membrane / p38MAPK cascade / monoatomic cation transmembrane transport / fatty acid oxidation / ATPase-coupled transmembrane transporter activity / potassium channel activity / protein secretion / ABC-type transporter activity / potassium channel regulator activity / heart morphogenesis / fatty acid transport / ATP metabolic process / presynaptic active zone membrane / skeletal muscle tissue development / T-tubule / potassium ion transmembrane transport / negative regulation of blood pressure / response to endoplasmic reticulum stress / regulation of heart rate / sarcomere / cellular response to calcium ion / blood vessel diameter maintenance / acrosomal vesicle / regulation of membrane potential / response to cytokine / kidney development / determination of adult lifespan / response to activity / response to ischemia / mitochondrion organization / calcium ion transmembrane transport / microglial cell activation / response to insulin / potassium ion transport / response to hydrogen peroxide / transmembrane transport / sarcolemma / regulation of blood pressure / response to estrogen / vasodilation / MAPK cascade / cellular response to xenobiotic stimulus / heart development / presynapse / gene expression
Similarity search - Function
Potassium channel, inwardly rectifying, Kir6.1 / ATP-binding cassette subfamily C member 9 / : / Sulphonylurea receptor / Potassium channel, inwardly rectifying, transmembrane domain / Inward rectifier potassium channel transmembrane domain / Potassium channel, inwardly rectifying, Kir, cytoplasmic / Potassium channel, inwardly rectifying, Kir / Inward rectifier potassium channel, C-terminal / Inward rectifier potassium channel C-terminal domain ...Potassium channel, inwardly rectifying, Kir6.1 / ATP-binding cassette subfamily C member 9 / : / Sulphonylurea receptor / Potassium channel, inwardly rectifying, transmembrane domain / Inward rectifier potassium channel transmembrane domain / Potassium channel, inwardly rectifying, Kir, cytoplasmic / Potassium channel, inwardly rectifying, Kir / Inward rectifier potassium channel, C-terminal / Inward rectifier potassium channel C-terminal domain / : / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / Immunoglobulin E-set / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / : / ATP-binding cassette sub-family C member 9 / ATP-sensitive inward rectifier potassium channel 8
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsSung, M.W. / Shyng, S.L.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)R01DK066485-13 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2021
Title: Vascular K channel structural dynamics reveal regulatory mechanism by Mg-nucleotides.
Authors: Min Woo Sung / Zhongying Yang / Camden M Driggers / Bruce L Patton / Barmak Mostofian / John D Russo / Daniel M Zuckerman / Show-Ling Shyng /
Abstract: Vascular tone is dependent on smooth muscle K channels comprising pore-forming Kir6.1 and regulatory SUR2B subunits, in which mutations cause Cantú syndrome. Unique among K isoforms, they lack ...Vascular tone is dependent on smooth muscle K channels comprising pore-forming Kir6.1 and regulatory SUR2B subunits, in which mutations cause Cantú syndrome. Unique among K isoforms, they lack spontaneous activity and require Mg-nucleotides for activation. Structural mechanisms underlying these properties are unknown. Here, we determined cryogenic electron microscopy structures of vascular K channels bound to inhibitory ATP and glibenclamide, which differ informatively from similarly determined pancreatic K channel isoform (Kir6.2/SUR1). Unlike SUR1, SUR2B subunits adopt distinct rotational "propeller" and "quatrefoil" geometries surrounding their Kir6.1 core. The glutamate/aspartate-rich linker connecting the two halves of the SUR-ABC core is observed in a quatrefoil-like conformation. Molecular dynamics simulations reveal MgADP-dependent dynamic tripartite interactions between this linker, SUR2B, and Kir6.1. The structures captured implicate a progression of intermediate states between MgADP-free inactivated, and MgADP-bound activated conformations wherein the glutamate/aspartate-rich linker participates as mobile autoinhibitory domain, suggesting a conformational pathway toward K channel activation.
History
DepositionApr 20, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 13, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 26, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 30, 2024Group: Data collection / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_3d_fitting_list / em_admin / pdbx_entry_details / pdbx_initial_refinement_model / pdbx_modification_feature
Item: _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id ..._em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type / _em_admin.last_update / _pdbx_entry_details.has_protein_modification

-
Structure visualization

Movie
  • Deposited structure unit
  • Imaged by Jmol
  • Download
  • Superimposition on EM map
  • EMDB-23882
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: ATP-sensitive inward rectifier potassium channel 8
B: ATP-sensitive inward rectifier potassium channel 8
C: ATP-sensitive inward rectifier potassium channel 8
D: ATP-sensitive inward rectifier potassium channel 8
E: Isoform SUR2B of ATP-binding cassette sub-family C member 9
G: Isoform SUR2B of ATP-binding cassette sub-family C member 9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)544,49614
Polymers541,0736
Non-polymers3,4248
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

-
Components

#1: Protein
ATP-sensitive inward rectifier potassium channel 8 / Inward rectifier K(+) channel Kir6.1 / Potassium channel / inwardly rectifying subfamily J member 8 / uKATP-1


Mass: 48023.871 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Kcnj8 / Production host: Chlorocebus aethiops (grivet) / References: UniProt: Q63664
#2: Protein Isoform SUR2B of ATP-binding cassette sub-family C member 9 / Sulfonylurea receptor 2


Mass: 174488.562 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Abcc9, Sur2 / Production host: Chlorocebus aethiops (grivet) / References: UniProt: Q63563
#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#4: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#5: Chemical
ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP, energy-carrying molecule*YM
Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

ComponentName: Vascular KATP channel: Kir6.1 SUR2B quatrefoil-like conformation 2
Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Molecular weightValue: 0.889 MDa / Experimental value: YES
Source (natural)Organism: Rattus norvegicus (Norway rat)
Source (recombinant)Organism: Chlorocebus aethiops (grivet)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid type: Quantifoil R2/1
VitrificationCryogen name: ETHANE

-
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: SPOT SCAN
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

-
Processing

EM software
IDNameVersionCategory
2SerialEMimage acquisition
7Cootmodel fitting
9PHENIXmodel refinement
13RELION33D reconstruction
CTF correctionType: NONE
3D reconstructionResolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 22038 / Symmetry type: POINT
Atomic model buildingPDB-ID: 6BAA
Accession code: 6BAA / Source name: PDB / Type: experimental model

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more