Structural highlights
Function
[C9QXJ2_ECOD1] Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell (By similarity).[SAAS:SAAS001185_004_016395][HAMAP-Rule:MF_00115]
Publication Abstract from PubMed
The crystal structure of the cytoplasmic domain (CTD) from the mechanosensitive channel of large conductance (MscL) in E. coli has been determined at 1.45 A resolution. This domain forms a pentameric coiled coil similar to that observed in the structure of MscL from M. tuberculosis and also found in the Cartilage Oligomeric Matrix Protein (COMPcc). It contains canonical hydrophobic and atypical ionic interactions compared to previously characterized coiled coil structures. Thermodynamic analysis indicates that while the free EcMscL-CTD is less stable than other coiled coils, it is likely to remain folded in context of the full-length channel.
Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance.,Walton TA, Rees DC Protein Sci. 2013 Aug 29. doi: 10.1002/pro.2360. PMID:24038743[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Walton TA, Rees DC. Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance. Protein Sci. 2013 Aug 29. doi: 10.1002/pro.2360. PMID:24038743 doi:10.1002/pro.2360
