title: Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.
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.
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Valentina
authors.initials: V
authors.lastname: Zorzini
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Lieven
authors.initials: L
authors.lastname: Buts
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Mike
authors.initials: M
authors.lastname: Sleutel
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Abel
authors.initials: A
authors.lastname: Garcia-Pino
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Ariel
authors.initials: A
authors.lastname: Talavera
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Sarah
authors.initials: S
authors.lastname: Haesaerts
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Henri
authors.initials: H
authors.lastname: De Greve
authors.affiliation: Department of Microbiology and Immunology, Dartmouth Medical School, Hanover, NH 03755, USA.
authors.forename: Ambrose
authors.initials: A
authors.lastname: Cheung
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium Molecular Recognition Unit, Department of Structural Biology, VIB, Pleinlaan 2, 1050 Brussels, Belgium.
authors.forename: Nico A J
authors.initials: NA
authors.lastname: van Nuland
authors.affiliation: 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.
authors.forename: Remy
authors.initials: R
authors.lastname: Loris
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D001427:Bacterial Toxins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000737:chemistry; D004722:Endoribonucleases / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D058767:Protein Unfolding; D013211:Staphylococcus aureus
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C422955:MazF protein, E coli; D004722:Endoribonucleases
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