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- PDB-6ci1: The Structure of Full-Length Kv Beta 2.1 Determined by Cryogenic ... -

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Entry
Database: PDB / ID: 6ci1
TitleThe Structure of Full-Length Kv Beta 2.1 Determined by Cryogenic Electron Microscopy
ComponentsVoltage-gated potassium channel subunit beta-2
KeywordsOXIDOREDUCTASE / Kv Channel / Regulator / Complex
Function / homologyNADP-dependent oxidoreductase domain / Potassium channel, voltage-dependent, beta subunit, KCNAB / Potassium channel, voltage-dependent, beta subunit, KCNAB-related / Neutrophil degranulation / Voltage gated Potassium channels / Potassium channel, voltage-dependent, beta subunit, KCNAB2 / Aldo/keto reductase family / NADP-dependent oxidoreductase domain superfamily / pinceau fiber / NADPH oxidation ...NADP-dependent oxidoreductase domain / Potassium channel, voltage-dependent, beta subunit, KCNAB / Potassium channel, voltage-dependent, beta subunit, KCNAB-related / Neutrophil degranulation / Voltage gated Potassium channels / Potassium channel, voltage-dependent, beta subunit, KCNAB2 / Aldo/keto reductase family / NADP-dependent oxidoreductase domain superfamily / pinceau fiber / NADPH oxidation / potassium channel complex / regulation of protein localization to cell surface / aldo-keto reductase (NADP) activity / juxtaparanode region of axon / regulation of potassium ion transmembrane transport / potassium channel regulator activity / Oxidoreductases, Acting on the CH-OH group of donors, With NAD+ or NADP+ as acceptor / myoblast differentiation / voltage-gated potassium channel activity / extrinsic component of cytoplasmic side of plasma membrane / protein heterooligomerization / ion channel binding / oxidation-reduction process / cytoskeleton / cell junction / synapse / neuron projection / axon / cytosol / Voltage-gated potassium channel subunit beta-2
Function and homology information
Specimen sourceRattus norvegicus (Norway rat)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 4.9 Å resolution
AuthorsStagg, S.M. / Spear, J.M. / Mendez, J.H.
CitationJournal: To Be Published
Title: The Structure of Full-Length Kv Beta 2.1 Determined by Cryogenic Electron Microscopy
Authors: Stagg, S.M. / Spear, J.M. / Mendez, J.H.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Feb 23, 2018 / Release: Feb 27, 2019

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Structure visualization

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Assembly

Deposited unit
A: Voltage-gated potassium channel subunit beta-2
B: Voltage-gated potassium channel subunit beta-2
C: Voltage-gated potassium channel subunit beta-2
D: Voltage-gated potassium channel subunit beta-2
E: Voltage-gated potassium channel subunit beta-2
F: Voltage-gated potassium channel subunit beta-2
G: Voltage-gated potassium channel subunit beta-2
H: Voltage-gated potassium channel subunit beta-2


Theoretical massNumber of molelcules
Total (without water)291,5288
Polyers291,5288
Non-polymers00
Water0
1


TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein/peptide
Voltage-gated potassium channel subunit beta-2 / / K(+) channel subunit beta-2 / Kv-beta-2 / Coordinate model: Cα atoms only


Mass: 36440.992 Da / Num. of mol.: 8 / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Kcnab2, Ckbeta2, Kcnb3 / Production host: Escherichia coli (E. coli)
References: UniProt: P62483, Oxidoreductases, Acting on the CH-OH group of donors, With NAD+ or NADP+ as acceptor

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Experimental details

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Experiment

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

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Sample preparation

ComponentName: Octamer of Kv Beta / Type: COMPLEX / Entity ID: 1 / Source: RECOMBINANT
Source (natural)Organism: Rattus norvegicus (Norway rat)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
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
MicroscopyMicroscope model: 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: 60 e/Å2 / Film or detector model: DIRECT ELECTRON DE-20 (5k x 3k)

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Processing

EM software
IDNameCategory
7UCSF Chimeramodel fitting
13MDFFmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: D4
3D reconstructionResolution: 4.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 24809 / Symmetry type: POINT
Atomic model buildingRef protocol: FLEXIBLE FIT / Ref space: REAL

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