ArticleActa crystallographica. Section D, Biological crystallography2014
Structure of archaerhodopsin-2 at 1.8 Å resolution.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Crystallographic insights into lipid-membrane protein interactions in microbial rhodopsins.Frontiers in molecular biosciences · 2024Article
- QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins.Nature communications · 2022Article
- Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.Nature communications · 2021Article
- NeoR, a near-infrared absorbing rhodopsin.Nature communications · 2020Article
- Redshifted and Near-infrared Active Analog Pigments Based upon Archaerhodopsin-3.Photochemistry and photobiology · 2019Article
- a-ARM: Automatic Rhodopsin Modeling with Chromophore Cavity Generation, Ionization State Selection, and External Counterion Placement.Journal of chemical theory and computation · 2019Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- X-ray structure analysis of bacteriorhodopsin at 1.3 Å resolution.Scientific reports · 2018Article
- Energetics and dynamics of a light-driven sodium-pumping rhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Directed Evolution of a Bright Near-Infrared Fluorescent Rhodopsin Using a Synthetic Chromophore.Cell chemical biology · 2017Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Archaerhodopsin-2 (aR2), the sole protein found in the claret membrane of Halorubrum sp. Aus-2, functions as a light-driven proton pump. In this study, structural analysis of aR2 was performed using a novel three-dimensional crystal prepared by the successive fusion of claret membranes. The crystal is made up of stacked membranes, in each of which aR2 trimers are arranged on a hexagonal lattice. This lattice structure resembles that found in the purple membrane of H. salinarum, except that lipid molecules trapped within the trimeric structure are not distributed with perfect threefold symmetry. Nonetheless, diffraction data at 1.8 Å resolution provide accurate structural information about functionally important residues. It is shown that two glutamates in the proton-release channel form a paired structure that is maintained by a low-barrier hydrogen bond. Although the structure of the proton-release pathway is highly conserved among proton-pumping archaeal rhodopsins, aR2 possesses the following peculiar structural features: (i) the motional freedom of the tryptophan residue that makes contact with the C13 methyl group of retinal is restricted, affecting the formation/decay kinetics of the L state, and (ii) the N-terminal polypeptide folds into an Ω-loop, which may play a role in organizing the higher-order structure.
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