|Entry||Database: PDB / ID: 6uwm|
|Title||Single particle cryo-EM structure of KvAP|
|Components||Voltage-gated potassium channel|
|Keywords||TRANSPORT PROTEIN / voltage-gated potassium channel / non-domain-swapped|
|Function / homology||Ion transport domain / Voltage-gated potassium channel / Ion transport protein / voltage-gated potassium channel activity / regulation of ion transmembrane transport / voltage-gated potassium channel complex / identical protein binding / Voltage-gated potassium channel|
Function and homology information
|Biological species||Aeropyrum pernix (archaea)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.9 Å|
|Authors||Tao, X. / MacKinnon, R.|
|Funding support|| United States, 1items |
|Citation||Journal: Elife / Year: 2019|
Title: Cryo-EM structure of the KvAP channel reveals a non-domain-swapped voltage sensor topology.
Authors: Xiao Tao / Roderick MacKinnon /
Abstract: Conductance in voltage-gated ion channels is regulated by membrane voltage through structural domains known as voltage sensors. A single structural class of voltage sensor domain exists, but two ...Conductance in voltage-gated ion channels is regulated by membrane voltage through structural domains known as voltage sensors. A single structural class of voltage sensor domain exists, but two different modes of voltage sensor attachment to the pore occur in nature: domain-swapped and non-domain-swapped. Since the more thoroughly studied Kv1-7, Nav and Cav channels have domain-swapped voltage sensors, much less is known about non-domain-swapped voltage-gated ion channels. In this paper, using cryo-EM, we show that KvAP from has non-domain-swapped voltage sensors as well as other unusual features. The new structure, together with previous functional data, suggests that KvAP and the Shaker channel, to which KvAP is most often compared, probably undergo rather different voltage-dependent conformational changes when they open.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: Voltage-gated potassium channel
C: Voltage-gated potassium channel
B: Voltage-gated potassium channel
D: Voltage-gated potassium channel
Mass: 31649.207 Da / Num. of mol.: 4 / Fragment: UNP residues 25-295
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aeropyrum pernix (archaea) / Gene: APE_0955 / Plasmid: pET28a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q9YDF8
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Source (recombinant)||Organism: Escherichia coli BL21(DE3) (bacteria) / Plasmid: pET28a|
|Buffer solution||pH: 8|
|Specimen||Conc.: 6 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: KvAP in complex with 6E1 Fab|
|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
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 magnification: 29000 X / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE|
|Specimen holder||Cryogen: NITROGEN / Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Image recording||Average exposure time: 10 sec. / Electron dose: 75 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 8000|
|Image scans||Movie frames/image: 50 / Used frames/image: 1-50|
|CTF correction||Type: NONE|
|Particle selection||Num. of particles selected: 1800000|
|Symmetry||Point symmetry: C4 (4 fold cyclic)|
|3D reconstruction||Resolution: 5.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 67000 / Num. of class averages: 2 / Symmetry type: POINT|
|Atomic model building||Protocol: RIGID BODY FIT / Space: REAL|
|Atomic model building|
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