Document Type
Article
Publication Date
3-19-2014
Publication Title
Nucleic Acids Research
Department
Geisel School of Medicine
Abstract
The Staphylococcus aureus genome contains three toxin-antitoxin modules, including one mazEF module, SamazEF. Using an on-column separation protocol we are able to obtain large amounts of wild-type SaMazF toxin. The protein is well-folded and highly resistant against thermal unfolding but aggregates at elevated temperatures. Crystallographic and nuclear magnetic resonance (NMR) solution studies show a well-defined dimer. Differences in structure and dynamics between the X-ray and NMR structural ensembles are found in three loop regions, two of which undergo motions that are of functional relevance. The same segments also show functionally relevant dynamics in the distantly related CcdB family despite divergence of function. NMR chemical shift mapping and analysis of residue conservation in the MazF family suggests a conserved mode for the inhibition of MazF by MazE.
DOI
10.1093/nar/gku266
Dartmouth Digital Commons Citation
Zorzini, Valentina; Buts, Lieven; Sleutel, Mike; Garcia-Pino, Abel; Talavera, Ariel; Haesaerts, Sarah; De Greve, Henri; Cheung, Ambrose; van Nuland, Nico A. J.; and Loris, Remy, "Structural and Biophysical Characterization of Staphylococcus Aureus SaMazF Shows Conservation of Functional Dynamics" (2014). Dartmouth Scholarship. 3868.
https://digitalcommons.dartmouth.edu/facoa/3868
