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

Article, Other literature type English OPEN
Maurer, Joshua A. ; Elmore, Donald E. ; Clayton, Daniel ; Xiong, Li ; Lester, Henry A. ; Dougherty, Dennis A. (2008)
  • Publisher: The Biophysical Society
  • Journal: Biophysical Journal, volume 94, issue 12, pages 4,662-4,667 (issn: 0006-3495)
  • Related identifiers: doi: 10.1529/biophysj.107.127365
  • Subject: Channels, Receptors, and Electrical Signaling | Biophysics
    mesheuropmc: fungi

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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