High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer.
Details
Serval ID
serval:BIB_B5652DE74C88
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer.
Journal
Structure
ISSN
1878-4186 (Electronic)
ISSN-L
0969-2126
Publication state
Published
Issued date
02/01/2018
Peer-reviewed
Oui
Volume
26
Number
1
Pages
20-27.e3
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
Abstract
Eukaryotic cyclic nucleotide-modulated channels perform their diverse physiological roles by opening and closing their pores to ions in response to cyclic nucleotide binding. We here present a structural model for the cyclic nucleotide-modulated potassium channel homolog from Mesorhizobium loti, MloK1, determined from 2D crystals in the presence of lipids. Even though crystals diffract electrons to only ∼10 Å, using cryoelectron microscopy (cryo-EM) and recently developed computational methods, we have determined a 3D map of full-length MloK1 in the presence of cyclic AMP (cAMP) at ∼4.5 Å isotropic 3D resolution. The structure provides a clear picture of the arrangement of the cyclic nucleotide-binding domains with respect to both the pore and the putative voltage sensor domains when cAMP is bound, and reveals a potential gating mechanism in the context of the lipid-embedded channel.
Keywords
Bacterial Proteins/chemistry, Bacterial Proteins/genetics, Bacterial Proteins/metabolism, Binding Sites, Caenorhabditis elegans Proteins/chemistry, Caenorhabditis elegans Proteins/genetics, Caenorhabditis elegans Proteins/metabolism, Cloning, Molecular, Cryoelectron Microscopy/methods, Cyclic AMP/chemistry, Cyclic AMP/metabolism, Escherichia coli/genetics, Escherichia coli/metabolism, Gene Expression, Genetic Vectors/chemistry, Genetic Vectors/metabolism, Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/chemistry, Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/genetics, Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels/metabolism, Image Processing, Computer-Assisted/methods, Ion Channel Gating, Ion Channels/chemistry, Ion Channels/genetics, Ion Channels/metabolism, Lipid Bilayers/chemistry, Lipid Bilayers/metabolism, Mesorhizobium/chemistry, Mesorhizobium/metabolism, Models, Molecular, Potassium/chemistry, Potassium/metabolism, Potassium Channels/chemistry, Potassium Channels/genetics, Potassium Channels/metabolism, Potassium Channels, Voltage-Gated/chemistry, Potassium Channels, Voltage-Gated/genetics, Potassium Channels, Voltage-Gated/metabolism, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Recombinant Proteins/chemistry, Recombinant Proteins/genetics, Recombinant Proteins/metabolism, Structural Homology, Protein, Thermodynamics, 2D crystals, CNBD, MloK1, MlotiK1, cryoelectron microscopy, cytoplasmic domains, electron crystallography, membrane protein, potassium channel, voltage sensor
Pubmed
Web of science
Open Access
Yes
Create date
09/06/2023 16:02
Last modification date
08/07/2023 6:50
Usage data
