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Published June 15, 2008 | public
Journal Article

Confirming the Revised C-Terminal Domain of the MscL Crystal Structure

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.

Additional Information

© 2008 The Biophysical Society. Received 6 December 2007, Accepted 23 January 2008, Available online 6 January 2009. This work was partially supported by the National Institutes of Health Program Project Grant GM-62532. Additional support was provided by the Office of the Dean at Wellesley College. Joshua A. Maurer and Donald E. Elmore contributed equally to this work.

Additional details

Created:
August 19, 2023
Modified:
October 25, 2023