ArticleBiophysical journal2008
Confirming the revised C-terminal domain of the MscL crystal structure.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural investigation of MscL gating using experimental data and coarse grained MD simulations.PLoS computational biology · 2012Article
- Conserved motifs in mechanosensitive channels MscL and MscS.European biophysics journal : EBJ · 2009Article
- Mechanosensitive channels: insights from continuum-based simulations.Cell biochemistry and biophysics · 2008Review
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Authors and funding
6 authors.
Funding
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 alpha-helical bundle conformation similar to that observed in the E. coli MscL model and the revised Tb-MscL crystal structure.
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