ArticleStructure (London, England : 1993)2007
The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution.
Article in Structure (London, England : 1993), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed.
- DM: a simple solution to suppress air-water interface interactions in cryo-EM.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of properties, mechanisms, and channelopathy of cyclic nucleotide-gated channels.Channels (Austin, Tex.) · 2023Review
- Objective crystallographic symmetry classifications of a noisy crystal pattern with strong Fedorov-type pseudosymmetries and its optimal image-quality enhancement.Acta crystallographica. Section A, Foundations and advances · 2022Article
- Sample Preparation and Data Collection for Electron Crystallographic Studies on Membrane Protein Structures and Lipid-Protein Interaction.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM.Nature communications · 2019Article
- Minimal molecular determinants of isoform-specific differences in efficacy in the HCN channel family.The Journal of general physiology · 2018Article
- Article
- Ligand binding and activation properties of the purified bacterial cyclic nucleotide-gated channel SthK.The Journal of general physiology · 2018Article
- A Quantitative Model for cAMP Binding to the Binding Domain of MloK1.Biophysical journal · 2016Article
- Real-time visualization of conformational changes within single MloK1 cyclic nucleotide-modulated channels.Nature communications · 2016Article
- Two-Dimensional Crystallization Procedure, from Protein Expression to Sample Preparation.BioMed research international · 2015Review
- Determinants of ligand selectivity in a cyclic nucleotide-regulated potassium channel.The Journal of general physiology · 2014Article
- A KcsA/MloK1 chimeric ion channel has lipid-dependent ligand-binding energetics.The Journal of biological chemistry · 2014Article
- Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.Nature communications · 2014Article
- A novel dimerization interface of cyclic nucleotide binding domain, which is disrupted in presence of cAMP: implications for CNG channels gating.Journal of molecular modeling · 2012Article
- Gating of the MlotiK1 potassium channel involves large rearrangements of the cyclic nucleotide-binding domains.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy.The Journal of biological chemistry · 2011Article
- Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- A 3.5-nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy.The Journal of biological chemistry · 2010Article
- Cloning and functional expression of an MscL ortholog from Rhizobium etli: characterization of a mechanosensitive channel.The Journal of membrane biology · 2010Article
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Abstract
The gating ring of cyclic nucleotide-modulated channels is proposed to be either a two-fold symmetric dimer of dimers or a four-fold symmetric tetramer based on high-resolution structure data of soluble cyclic nucleotide-binding domains and functional data on intact channels. We addressed this controversy by obtaining structural data on an intact, full-length, cyclic nucleotide-modulated potassium channel, MloK1, from Mesorhizobium loti, which also features a putative voltage-sensor. We present here the 3D single-particle structure by transmission electron microscopy and the projection map of membrane-reconstituted 2D crystals of MloK1 in the presence of cAMP. Our data show a four-fold symmetric arrangement of the CNBDs, separated by discrete gaps. A homology model for full-length MloK1 suggests a vertical orientation for the CNBDs. The 2D crystal packing in the membrane-embedded state is compatible with the S1-S4 domains in the vertical "up" state.
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