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- PDB-4chv: The electron crystallography structure of the cAMP-bound potassiu... -
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Basic information
Entry | Database: PDB / ID: 4chv | ||||||
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Title | The electron crystallography structure of the cAMP-bound potassium channel MloK1 | ||||||
![]() | CYCLIC NUCLEOTIDE-GATED POTASSIUM CHANNEL MLL3241 | ||||||
![]() | TRANSPORT / 2DX / VOLTAGE GATED POTASSIUM CHANNEL / CNBD / 2D CRYSTAL | ||||||
Function / homology | ![]() intracellular cyclic nucleotide activated cation channel complex / intracellularly cGMP-activated cation channel activity / intracellularly cAMP-activated cation channel activity / potassium channel activity / cGMP binding / cAMP binding / protein-containing complex binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON CRYSTALLOGRAPHY / electron crystallography / cryo EM / Resolution: 7 Å | ||||||
![]() | Kowal, J. / Chami, M. / Baumgartner, P. / Arheit, M. / Chiu, P.L. / Rangl, M. / Scheuring, S. / Schroeder, G.F. / Nimigean, C.M. / Stahlberg, H. | ||||||
![]() | ![]() Title: Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1. Authors: Julia Kowal / Mohamed Chami / Paul Baumgartner / Marcel Arheit / Po-Lin Chiu / Martina Rangl / Simon Scheuring / Gunnar F Schröder / Crina M Nimigean / Henning Stahlberg / ![]() ![]() ![]() ![]() Abstract: Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly ...Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. Here we report ligand-induced conformational changes in full-length MloK1, a cyclic nucleotide-modulated potassium channel from the bacterium Mesorhizobium loti, analysed by electron crystallography and atomic force microscopy. Upon cAMP binding, the cyclic nucleotide-binding domains move vertically towards the membrane, and directly contact the S1-S4 voltage sensor domains. This is accompanied by a significant shift and tilt of the voltage sensor domain helices. In both states, the inner pore-lining helices are in an 'open' conformation. We propose a mechanism in which ligand binding can favour pore opening via a direct interaction between the cyclic nucleotide-binding domains and voltage sensors. This offers a simple mechanistic hypothesis for the coupling between ligand gating and voltage sensing in eukaryotic HCN channels. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 254.4 KB | Display | ![]() |
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PDB format | ![]() | 207.6 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 866.4 KB | Display | ![]() |
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Full document | ![]() | 977.3 KB | Display | |
Data in XML | ![]() | 55.7 KB | Display | |
Data in CIF | ![]() | 80.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2526MC ![]() 2527C ![]() 4chwC C: citing same article ( M: map data used to model this data |
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Similar structure data | |
EM raw data | ![]() Data size: 11.6 Data #1: Potassium channel MloK1 with cAMP ligand [micrographs - single frame] Data #2: Potassium channel MloK1 without cAMP ligand [micrographs - single frame]) |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 38595.164 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: CAMP PRESENT IN BUFFER / Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON CRYSTALLOGRAPHY |
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EM experiment | Aggregation state: 2D ARRAY / 3D reconstruction method: electron crystallography |
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Sample preparation
Component | Name: MLOK1 WITH CAMP / Type: COMPLEX |
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Buffer solution | Name: 20 MM KCL, 1 MM BACL2, 1 MM EDTA, 20 MM TRIS, 0.2 MM CAMP pH: 7.6 Details: 20 MM KCL, 1 MM BACL2, 1 MM EDTA, 20 MM TRIS, 0.2 MM CAMP |
Specimen | Conc.: 1.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Details: HOLEY CARBON |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
-Data collection
Microscopy | Model: FEI/PHILIPS CM200FEG / Date: Mar 1, 2012 |
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Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 50000 X / Nominal defocus max: 3077 nm / Nominal defocus min: 655 nm / Cs: 2 mm |
Specimen holder | Temperature: 85 K / Tilt angle max: 46 ° / Tilt angle min: 0 ° |
Image recording | Electron dose: 5 e/Å2 / Film or detector model: KODAK SO-163 FILM |
Image scans | Num. digital images: 78 |
Radiation | Scattering type: electron |
Radiation wavelength | Relative weight: 1 |
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Processing
3D reconstruction | Resolution: 7 Å / Resolution method: OTHER / Symmetry type: 2D CRYSTAL | ||||||||||||
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Refinement | Highest resolution: 7 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 7 Å
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