4lku
From Proteopedia
Structure of the C-terminal domain of the E. coli mechanosensitive channel of large conductance
Structural highlights
FunctionMSCL_ECOLI Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. Participates in the regulation of osmotic pressure changes within the cell. Opens at a pressure just below that which would cause cell disruption and death. The force required to trigger channel opening depends on the membrane lipids composition.[1] [2] [3] [4] [5] Publication Abstract from PubMedThe 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||
