4LKU
Structure of the C-terminal domain of the E. coli mechanosensitive channel of large conductance
Summary for 4LKU
Entry DOI | 10.2210/pdb4lku/pdb |
Descriptor | Large-conductance mechanosensitive channel (2 entities in total) |
Functional Keywords | pentamer, transport protein |
Biological source | Escherichia coli |
Total number of polymer chains | 5 |
Total formula weight | 16188.07 |
Authors | Walton, T.A.,Rees, D.C. (deposition date: 2013-07-08, release date: 2013-10-02, Last modification date: 2024-02-28) |
Primary citation | Walton, T.A.,Rees, D.C. Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance. Protein Sci., 22:1592-1601, 2013 Cited by PubMed Abstract: 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 Å 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. PubMed: 24038743DOI: 10.1002/pro.2360 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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