Crystal Structure of Cruxrhodopsin-3 from Haloarcula vallismortis
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چکیده
منابع مشابه
Crystal Structure of Cruxrhodopsin-3 from Haloarcula vallismortis
Cruxrhodopsin-3 (cR3), a retinylidene protein found in the claret membrane of Haloarcula vallismortis, functions as a light-driven proton pump. In this study, the membrane fusion method was applied to crystallize cR3 into a crystal belonging to space group P321. Diffraction data at 2.1 Å resolution show that cR3 forms a trimeric assembly with bacterioruberin bound to the crevice between neighbo...
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In this study, the feasibility of cruxrhodopsin (CR) production as a multifunctional nanoparticle was investigated and optimized by Halorculasp. IRU1, a novel halophile Archaea isolated from Urmia Lake, Iran in batch experiments. In this case, Taguchi method was used for effect measurement of three important factors (petrochemical wastewater, yeast extract and KH2PO4) on CR production. Results ...
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Bacteriorhodopsins are a large family of seven-helical transmembrane proteins that function as light-driven proton pumps. Here, we present the crystal structure of a new member of the family, Haloarcula marismortui bacteriorhodopsin I (HmBRI) D94N mutant, at the resolution of 2.5 Å. While the HmBRI retinal-binding pocket and proton donor site are similar to those of other archaeal proton pumps,...
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ژورنال
عنوان ژورنال: PLoS ONE
سال: 2014
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0108362