|Entry||Database: EMDB / ID: EMD-20924|
|Title||Single particle cryo-EM structure of KvAP|
|Sample||KvAP-6E1 Fab complex:|
KvAP / 6E1 Fab / Voltage-gated potassium channel
|Function / homology||Ion transport domain / Voltage-gated potassium channel / 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) / unidentified (others)|
|Method||single particle reconstruction / cryo EM / Resolution: 5.9 Å|
|Authors||Tao X / MacKinnon R|
|Funding support|| United States, 1 items |
|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.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_20924.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.028 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire KvAP-6E1 Fab complex
|Entire||Name: KvAP-6E1 Fab complex / Number of components: 4|
-Component #1: protein, KvAP-6E1 Fab complex
|Protein||Name: KvAP-6E1 Fab complex / Recombinant expression: No|
|Mass||Theoretical: 200 kDa|
-Component #2: protein, KvAP
|Protein||Name: KvAP / Details: KvAP tetramer / Recombinant expression: No|
|Mass||Theoretical: 130 kDa|
|Source||Species: Aeropyrum pernix (archaea)|
|Source (engineered)||Expression System: Escherichia coli BL21(DE3) (bacteria) / Vector: pET28a|
-Component #3: protein, 6E1 Fab
|Protein||Name: 6E1 Fab / Recombinant expression: No|
|Source||Species: unidentified (others)|
-Component #4: protein, Voltage-gated potassium channel
|Protein||Name: Voltage-gated potassium channel / Number of Copies: 4 / Recombinant expression: No|
|Mass||Theoretical: 31.649207 kDa|
|Source||Species: Aeropyrum pernix (archaea)|
|Source (engineered)||Expression System: Escherichia coli BL21(DE3) (bacteria)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||Specimen conc.: 6 mg/mL / pH: 8|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 295 K / Humidity: 100 % / Details: Blot for 4 seconds before plunging..|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 75 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 29000.0 X (nominal) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 800.0 - 2200.0 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Image acquisition||Number of digital images: 8000|
|Processing||Method: single particle reconstruction / Applied symmetry: C4 (4 fold cyclic) / Number of projections: 67000|
|3D reconstruction||Software: FREALIGN / Resolution: 5.9 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
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