Leptosphaeria rhodopsin: Bacteriorhodopsin-like proton pump from a eukaryote
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منابع مشابه
Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eukaryote.
Bacteriorhodopsin-like proteins provide archaea and eubacteria with a unique bioenergetic pathway comprising light-driven transmembrane proton translocation by a single retinal-binding protein. Recently, homologous proteins were found to perform photosensory functions in lower eukaryotes, but no active ion transport by eukaryotic rhodopsins was detected. By demonstrating light-driven proton pum...
متن کاملCarboxyl groups and the proton pump of bacteriorhodopsin.
The purple membrane isolated from Halobacterium halobium contains only a single protein, bacteriorhodopsin, which functions as a light-driven proton pump. Substantial structural information has been obtained which has led to specific models of protein structure in the membrane (Engelman et al., 1982; Huang et al., 1982; Agard & Stroud, 1982). The retinal chromophore of bacteriorhodopsin is boun...
متن کاملMolecular dynamics study of the proton pump cycle of bacteriorhodopsin.
Retinal isomerization reactions, which are functionally important in the proton pump cycle of bacteriorhodopsin, were studied by molecular dynamics simulations performed on the complete protein. Retinal isomerizations were simulated in situ to account for the effects of the retinal-protein interactions. The protein structure employed was that described in Nonella et al. [Nonella, M., Windemuth,...
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A homologue of type I rhodopsin was found in the unicellular Gloeobacter violaceus PCC7421, which is believed to be primitive because of the lack of thylakoids and peculiar morphology of phycobilisomes. The Gloeobacter rhodopsin (GR) gene encodes a polypeptide of 298 amino acids. This gene is localized alone in the genome unlike cyanobacterium Anabaena opsin, which is clustered together with 14...
متن کاملA microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties.
Rhodopsins possess retinal chromophore surrounded by seven transmembrane α-helices, are widespread in prokaryotes and in eukaryotes, and can be utilized as optogenetic tools. Although rhodopsins work as distinctly different photoreceptors in various organisms, they can be roughly divided according to their two basic functions, light-energy conversion and light-signal transduction. In microbes, ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2005
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0409659102