ArticleBiophysical journal2013
Structural insight into proteorhodopsin oligomers.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.Science advances · 2025Article
- Long-Time Scale Simulations Reveal Key Dynamics That Drive the Onset of the N State in the Proteorhodopsin Photocycle.The journal of physical chemistry. B · 2024Article
- Structural insights into the mechanism and dynamics of proteorhodopsin biogenesis and retinal scavenging.Nature communications · 2024Article
- Design of Soft Material Surfaces with Rationally Tuned Water Diffusivity.ACS central science · 2023Article
- Lipid membrane mimetics and oligomerization tune functional properties of proteorhodopsin.Biophysical journal · 2023Article
- Solid-State NMR Spectroscopy on Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin.Nature communications · 2021Article
- Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins.Biomolecules · 2020Review
- Electrostatic Environment of Proteorhodopsin Affects the pKa of Its Buried Primary Proton Acceptor.Biophysical journal · 2020Article
- Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories.Scientific reports · 2020Article
- Cryo-electron microscopic and X-ray crystallographic analysis of the light-driven proton pump proteorhodopsin reveals a pentameric assembly.Journal of structural biology: X · 2020Article
- X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin.Scientific reports · 2019Article
- Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- In vitro gene expression and detergent-free reconstitution of active proteorhodopsin in lipid vesicles.Experimental biology and medicine (Maywood, N.J.) · 2019Article
- Functionally Active Membrane Proteins Incorporated in Mesostructured Silica Films.Journal of the American Chemical Society · 2018Article
- Sparse Labeling PELDOR Spectroscopy on Multimeric Mechanosensitive Membrane Channels.Biophysical journal · 2017Article
- Proton-Based Structural Analysis of a Heptahelical Transmembrane Protein in Lipid Bilayers.Journal of the American Chemical Society · 2017Article
- Article
- Integrated In Silico Analysis of Pathway Designs for Synthetic Photo-Electro-Autotrophy.PloS one · 2016Article
- Characterization of an Unconventional Rhodopsin from the Freshwater Actinobacterium Rhodoluna lacicola.Journal of bacteriology · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligomerization has important functional implications for many membrane proteins. However, obtaining structural insight into oligomeric assemblies is challenging, as they are large and resist crystallization. We focus on proteorhodopsin (PR), a protein with seven transmembrane α-helices that was found to assemble to hexamers in densely packed lipid membrane, or detergent-solubilized environments. Yet, the structural organization and the subunit interface of these PR oligomers were unknown. We used site-directed spin-labeling together with electron spin-resonance lineshape and Overhauser dynamic nuclear polarization analysis to construct a model for the specific orientation of PR subunits within the hexameric complex. We found intersubunit distances to average 16 Å between neighboring 55 residues and that residues 177 are >20 Å apart from each other. These distance constraints show that PR has a defined and radial orientation within a hexamer, with the 55-site of the A-B loop facing the hexamer core and the 177-site of the E-F loop facing the hexamer exterior. Dynamic nuclear polarization measurements of the local solvent dynamics complement the electron spin-resonance-based distance analysis, by resolving whether protein surfaces at positions 55, 58, and 177 are exposed to solvent, or covered by protein-protein or protein-detergent contacts.
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