Published November 2013
| public
Journal Article
Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance
- Creators
- Walton, Troy A.
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Rees, Douglas C.
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.
Additional Information
© 2013 The Protein Society. Published by Wiley-Blackwell. Received 9 July 2013; Revised 12 August 2013; Accepted 14 August 2013. Grant sponsor: NIH; Grant number: 084211. The authors thank Jens Kaiser, Eric Johnson, and Matt Sazinsky for assistance with crystallography and members of the Rees laboratory for helpful comments. CD data were collected in the Beckman Institute Laser Resource Center. They also thank the Gordon and Betty Moore Foundation and the Beckman Institute for their generous support of the Molecular Observatory at Caltech. Portions of this research were carried out at the Stanford Synchrotron Radiation Lightsource (SSRL), a Directorate of SLAC National Accelerator Laboratory and an Office of Science User Facility operated for the US Department of Energy Office of Science by Stanford University. The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program (P41RR001209), and the National Institute of General Medical Sciences. Coordinates and structure factors have been deposited in the Protein Data Bank of the Research Collaboratory for Structural Bioinformatics, with ID 4LKU.Additional details
- PMCID
- PMC3831674
- Eprint ID
- 42246
- DOI
- 10.1002/pro.2360
- Resolver ID
- CaltechAUTHORS:20131105-094857416
- 084211
- NIH
- Gordon and Betty Moore Foundation
- Caltech Beckman Institute
- Department of Energy (DOE)
- P41RR001209
- NIH
- National Institute of General Medical Sciences
- Created
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2013-11-05Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field