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• W2085753726 endingPage "7950" @default.
• W2085753726 startingPage "7946" @default.
• W2085753726 abstract "The MotA protein of Escherichia coli is a component of the flagellar motors that functions in transmembrane proton conduction. Here, we report several features of MotA structure revealed by use of a mutagenesis-based approach. Single tryptophan residues were introduced at many positions within the four hydrophobic segments of MotA, and the effects on function were measured. Function was disrupted according to a periodic pattern that implies that the membrane-spanning segments are alpha-helices and that identifies the lipid-facing parts of each helix. The results support a hypothesis for MotA structure and mechanism in which water molecules form most of the proton-conducting pathway. The success of this approach in studying MotA suggests that it could be useful in structure-function studies of other integral membrane proteins." @default.
• W2085753726 created "2016-06-24" @default.
• W2085753726 creator A5035345393 @default.
• W2085753726 creator A5072799435 @default.
• W2085753726 creator A5079201187 @default.
• W2085753726 date "1995-08-15" @default.
• W2085753726 modified "2023-09-27" @default.
• W2085753726 title "Features of MotA proton channel structure revealed by tryptophan-scanning mutagenesis." @default.
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• W2085753726 doi "https://doi.org/10.1073/pnas.92.17.7946" @default.
• W2085753726 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/41263" @default.
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• W2085753726 hasPublicationYear "1995" @default.
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