ArticleBiophysical journal2015
In situ structural studies of Anabaena sensory rhodopsin in the E. coli membrane.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 67 citations in OpenAlex.
- Nuclear magnetic resonance of membrane proteins-Advances and opportunities.Current opinion in structural biology · 2026Review
- Dynamic structures of a membrane transporter in native cellular membranes.Science advances · 2025Article
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- Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025Review
- Solid-state NMR protocols for unveiling dynamics and (drug) interactions of membrane-bound proteins.Protein science : a publication of the Protein Society · 2025Article
- Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy.JACS Au · 2023Article
- Solid-state NMR structure determination of a membrane protein inScience advances · 2023Article
- Solid-State NMR Spectroscopy on Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.Nature protocols · 2021Article
- Conformational Dynamics of Light-Harvesting Complex II in a Native Membrane Environment.Biophysical journal · 2021Article
- Fake It 'Till You Make It-The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics.International journal of molecular sciences · 2020Review
- The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants.The Journal of biological chemistry · 2020Article
- Development of in vitro-grown spheroids as a 3D tumor model system for solid-state NMR spectroscopy.Journal of biomolecular NMR · 2020Article
- Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 inBiomolecules · 2020Article
- De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- DNP-Supported Solid-State NMR Spectroscopy of Proteins Inside Mammalian Cells.Angewandte Chemie (International ed. in English) · 2019Article
- Solid-state NMR spectroscopy based atomistic view of a membrane protein unfolding pathway.Nature communications · 2019Article
- An Inward-Rectifier Potassium Channel Coordinates the Properties of Biologically Derived Membranes.Biophysical journal · 2019Article
- Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR.Nature communications · 2018Article
- High-resolution NMR studies of antibiotics in cellular membranes.Nature communications · 2018Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Magic-angle spinning nuclear magnetic resonance is well suited for the study of membrane proteins in the nativelike lipid environment. However, the natural cellular membrane is invariably more complex than the proteoliposomes most often used for solid-state NMR (SSNMR) studies, and differences may affect the structure and dynamics of the proteins under examination. In this work we use SSNMR and other biochemical and biophysical methods to probe the structure of a seven-transmembrane helical photoreceptor, Anabaena sensory rhodopsin (ASR), prepared in the Escherichia coli inner membrane, and compare it to that in a bilayer formed by DMPC/DMPA lipids. We find that ASR is organized into trimers in both environments but forms two-dimensional crystal lattices of different symmetries. It favors hexagonal packing in liposomes, but may form a square lattice in the E. coli membrane. To examine possible changes in structure site-specifically, we perform two- and three-dimensional SSNMR experiments and analyze the differences in chemical shifts and peak intensities. Overall, this analysis reveals that the structure of ASR is largely conserved in the inner membrane of E. coli, with many of the important structural features of rhodopsins previously observed in ASR in proteoliposomes being preserved. Small, site-specific perturbations in protein structure that occur as a result of the membrane changes indicate that the protein can subtly adapt to its environment without large structural rearrangement.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.