Confirming the revised C-terminal domain of the MscL crystal structure.
Confirming the revised C-terminal domain of the MscL crystal structure.
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DOI：
10.1529/biophysj.107.127365
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发表时间：
2008-06
影响因子：
3.4
通讯作者：
J. A. Maurer;D. Elmore;D. Clayton;L. Xiong;H. Lester;D. Dougherty
中科院分区：
文献类型：
--
作者：
J. A. Maurer;D. Elmore;D. Clayton;L. Xiong;H. Lester;D. Dougherty
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 alpha-helical bundle conformation similar to that observed in the E. coli MscL model and the revised Tb-MscL crystal structure.
