PMID:7644518
| Citation |
Sharp, LL, Zhou, J and Blair, DF (1995) Features of MotA proton channel structure revealed by tryptophan-scanning mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 92:7946-50 |
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| 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. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; Cell Membrane/metabolism; Cell Movement; Cloning, Molecular; Escherichia coli/metabolism; Escherichia coli/physiology; Flagella/physiology; Macromolecular Substances; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Plasmids; Protein Structure, Secondary; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Restriction Mapping; Sequence Homology, Amino Acid; Tryptophan |
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