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Nucleic Acids Res. 2014 Jun;42(10):6709-25. doi: 10.1093/nar/gku266. Epub 2014 Apr 19.

Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.

Author information

1
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
2
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
3
Department of Microbiology and Immunology, Dartmouth Medical School, Hanover, NH 03755, USA.
4
Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium remy.loris@VIB-VUB.be.

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.

PMID:
24748664
PMCID:
PMC4041440
DOI:
10.1093/nar/gku266
[Indexed for MEDLINE]
Free PMC Article
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