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• W2021536633 endingPage "707" @default.
• W2021536633 startingPage "693" @default.
• W2021536633 abstract "Colicin Ia is a bactericidal protein of 626 amino acid residues that kills its target cell by forming a channel in the inner membrane; it can also form voltage-dependent channels in planar lipid bilayer membranes. The channel-forming activity resides in the carboxy-terminal domain of approximately 177 residues. In the crystal structure of the water-soluble conformation, this domain consists of a bundle of 10 alpha-helices, with eight mostly amphipathic helices surrounding a hydrophobic helical hairpin (helices H8-H9). We wish to know how this structure changes to form a channel in a lipid bilayer. Although there is evidence that the open channel has four transmembrane segments (H8, H9, and parts of H1 and H6-H7), their arrangement relative to the pore is largely unknown. Given the lack of a detailed structural model, it is imperative to better characterize the channel-lining protein segments. Here, we focus on a segment of 44 residues (573-616), which in the crystal structure comprises the H8-H9 hairpin and flanking regions. We mutated each of these residues to a unique cysteine, added the mutant colicins to the cis side of planar bilayers to form channels, and determined whether sulfhydryl-specific methanethiosulfonate reagents could alter the conduction of ions through the open channel. We found a pattern of reactivity consistent with parts of H8 and H9 lining the channel as alpha-helices, albeit rather short ones for spanning a lipid bilayer (12 residues). The effects of the reactions on channel conductance and selectivity tend to be greater for residues near the amino terminus of H8 and the carboxy terminus of H9, with particularly large effects for G577C, T581C, and G609C, suggesting that these residues may occupy a relatively constricted region near the cis end of the channel." @default.
• W2021536633 created "2016-06-24" @default.
• W2021536633 creator A5011798694 @default.
• W2021536633 creator A5056129248 @default.
• W2021536633 creator A5061348764 @default.
• W2021536633 date "2008-11-24" @default.
• W2021536633 modified "2023-10-15" @default.
• W2021536633 title "Identification of Channel-lining Amino Acid Residues in the Hydrophobic Segment of Colicin Ia" @default.
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• W2021536633 doi "https://doi.org/10.1085/jgp.200810042" @default.
• W2021536633 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2585860" @default.
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