|Title||Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.|
|Publication Type||Journal Article|
|Year of Publication||2014|
|Authors||Zorzini, V., L. Buts, M. Sleutel, A. Garcia-Pino, A. Talavera, S. Haesaerts, H. De Greve, A. Cheung, N. A. J. van Nuland, and R. Loris|
|Journal||Nucleic Acids Res|
|Date Published||2014 Jun|
|Keywords||Bacterial Proteins, Bacterial Toxins, Binding Sites, DNA-Binding Proteins, Endoribonucleases, Escherichia coli Proteins, Models, Molecular, Protein Conformation, Protein Unfolding, Staphylococcus aureus|
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.
|Alternate Journal||Nucleic Acids Res.|
|PubMed Central ID||PMC4041440|
Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.