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

Valentina Zorzini, Lieven Buts, Mike Sleutel, Abel Garcia Pino, Ariel Talavera Perez, Sarah Haesaerts, Henri De Greve, Ambrose Cheung, Nico Van Nuland, Remy Loris

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)6709-6725
Number of pages17
JournalNucleic Acids Res
Volume42
Publication statusPublished - 2014

Keywords

  • toxin-antitoxin module
  • persistence
  • ribonuclease
  • bacterial stress response
  • structural biology
  • bio-SAXS
  • small angle X-ray scatter
  • X-ray crystallography
  • bio-NMR
  • thermodynamic stability
  • protein stability
  • protein dynamics

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