Confirming the revised C-terminal domain of the MscL crystal structure |
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Authors: | Maurer Joshua A Elmore Donald E Clayton Daniel Xiong Li Lester Henry A Dougherty Dennis A |
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Institution: | * Department of Chemistry, Washington University, St. Louis, Missouri 63130 † Department of Chemistry, Wellesley College, Wellesley, Massachusetts 02482 ‡ Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125 § Division of Biology, California Institute of Technology, Pasadena, California 91125 |
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Abstract: | The structure of the C-terminal domain of the mechanosensitive channel of large conductance (MscL) has generated significant controversy. As a result, several structures have been proposed for this region: the original crystal structure (1MSL) of the Mycobacterium tuberculosis homolog (Tb), a model of the Escherichia coli homolog, and, most recently, a revised crystal structure of Tb-MscL (2OAR). To understand which of these structures represents a physiological conformation, we measured the impact of mutations to the C-terminal domain on the thermal stability of Tb-MscL using circular dichroism and performed molecular dynamics simulations of the original and the revised crystal structures of Tb-MscL. Our results imply that this region is helical and adopts an α-helical bundle conformation similar to that observed in the E. coli MscL model and the revised Tb-MscL crystal structure. |
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