Asymmetry of syringomycin E channel studied by polymer partitioning
نویسندگان
چکیده
منابع مشابه
Syringomycin E channel: a lipidic pore stabilized by lipopeptide?
Highly reproducible ion channels of the lipopeptide antibiotic syringomycin E demonstrate unprecedented involvement of the host bilayer lipids. We find that in addition to a pronounced influence of lipid species on the open-channel ionic conductance, the membrane lipids play a crucial role in channel gating. The effective gating charge, which characterizes sensitivity of the conformational equi...
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The nine-residue lipodepsipeptide syringomycin E, elaborated as a phytotoxin by Pseudomonas syringae pv. syringae B301D contains a 4-Cl-L-Thr-9 moiety where failure to chlorinate results in a 3-fold drop in biological activity. The proteins SyrB1 and SyrB2 encoded by the biosynthetic cluster are shown to act as a substrate and enzyme pair for SyrB2-mediated chlorination of the aminoacyl-S-enzym...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2007
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2007.01.063