Characterization of a Cyclic Nucleotide-Activated K(+) Channel and its Lipid Environment by Using Solid-State NMR Spectroscopy.
Chembiochem. 2013 Aug 16;
Authors: Cukkemane A, Baldus M
Abstract
Voltage-gated ion channels are large tetrameric multidomain membrane proteins that play crucial roles in various cellular transduction pathways. Because of their large size and domain-related mobility, structural characterization has proved challenging. We analyzed high-resolution solid-state NMR data on different isotope-labeled protein constructs of a bacterial cyclic nucleotide-activated K(+) channel (MlCNG) in lipid bilayers. We could identify the different subdomains of the 4×355 residue protein, such as the voltage-sensing domain and the cyclic nucleotide binding domain. Comparison to ssNMR data obtained on isotope-labeled cell membranes suggests a tight association of negatively charged lipids to the channel. We detected spectroscopic polymorphism that extends beyond the ligand binding site, and the corresponding protein segments have been associated with mutant channel types in eukaryotic systems. These findings illustrate the potential of ssNMR for structural investigations on large membrane-embedded proteins, even in the presence of local disorder.
PMID: 23956185 [PubMed - as supplied by publisher]
[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Acc Chem Res. 2013 Jul 5;
Authors: Opella SJ
Abstract
One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...
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[NMR paper] Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.
Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.
Biochim Biophys Acta. 2013 Feb;1828(2):824-33
Authors: Witte K, Olausson BE, Walrant A, Alves ID, Vogel A
...
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04-05-2013 10:53 AM
[NMR paper] Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment.
Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment.
Solution NMR spectroscopy for the determination of structures of membrane proteins in a lipid environment.
Methods Mol Biol. 2013;974:389-413
Authors: Arora A
Abstract
Several recent advancements have transformed solution NMR spectroscopy into a competitive, elegant, and eminently viable technique for determining the solution structures of membrane proteins at the level of atomic resolution. Once a good level of cell-based or...
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02-14-2013 02:37 PM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment
Abstract Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties with achieving proper folding, membrane insertion, and native-like post-translational modifications frequently disqualify bacterial expression systems. On the other hand, eukaryotic cell cultures can be prohibitively expensive. One of the viable alternatives,...
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01-22-2011 03:46 AM
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.
J Biomol NMR. 2011 Jan 19;
Authors: Fan Y, Shi L, Ladizhansky V, Brown LS
Overexpression of isotope-labeled multi-spanning eukaryotic membrane proteins for structural NMR studies is often challenging. On the one hand, difficulties...
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01-21-2011 01:22 AM
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Biochim Biophys Acta. 2010 Dec 28;
Authors: Penk A, Müller M, Scheidt HA, Langosch D, Huster D
The fusion of biological membranes is mediated by integral membrane proteins with ?-helical transmembrane segments. Additionally, those proteins are often modified by the covalent...
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01-05-2011 09:51 PM
[NMR paper] Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and
Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and obstructed random-walk perspective.
Related Articles Anomalous diffusion in a gel-fluid lipid environment: a combined solid-state NMR and obstructed random-walk perspective.
Biophys J. 2004 Oct;87(4):2456-69
Authors: Arnold A, Paris M, Auger M
Lateral diffusion is an essential process for the functioning of biological membranes. Solid-state nuclear magnetic resonance (NMR) is, a priori, a well-suited technique to study lateral diffusion within a heterogeneous...
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11-24-2010 10:01 PM
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel
Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers.
Protein Sci. 1998 Feb;7(2):342-8
Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA
The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...
Characterization of a Cyclic Nucleotide-Activated K(+) Channel and its Lipid Environment by Using Solid-State NMR Spectroscopy.
Linear Mode
