Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance

Autor:	Troy A, Walton, Douglas C, Rees
Rok vydání:	2013
Předmět:	Models Molecular Cytoplasm Protein Folding Protein Conformation Protein Stability Circular Dichroism Escherichia coli Proteins fungi Mycobacterium tuberculosis Articles Crystallography X-Ray Ion Channels Protein Structure Tertiary Bacterial Proteins Escherichia coli Thermodynamics
Zdroj:	Protein science : a publication of the Protein Society. 22(11)
ISSN:	1469-896X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::b2d1734e4e783febddaf6ae7cff0935b https://pubmed.ncbi.nlm.nih.gov/24038743 Zobrazit plný text záznamu Plný text