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Crystallization of the Staphylococcus aureus MazF mRNA interferase.

ABSTRACT: mazEF modules encode toxin-antitoxin pairs that are involved in the bacterial stress response through controlled and specific degradation of mRNA. Staphylococcus aureus MazF and MazE constitute a unique toxin-antitoxin module under regulation of the sigB operon. A MazF-type mRNA interferase is combined with an antitoxin of unknown fold. Crystals of S. aureus MazF (SaMazF) were grown in space group P2(1)2(1)2(1). The crystals diffracted to 2.1?Å resolution and are likely to contain two SaMazF dimers in the asymmetric unit.

SUBMITTER: Zorzini V

PROVIDER: S-EPMC3053169 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Crystallization of the Staphylococcus aureus MazF mRNA interferase.

Zorzini Valentina V Haesaerts Sarah S Donegan Niles P NP Fu Zhibiao Z Cheung Ambrose L AL van Nuland Nico A J NA Loris Remy R

Acta crystallographica. Section F, Structural biology and crystallization communications 20110225 Pt 3

mazEF modules encode toxin-antitoxin pairs that are involved in the bacterial stress response through controlled and specific degradation of mRNA. Staphylococcus aureus MazF and MazE constitute a unique toxin-antitoxin module under regulation of the sigB operon. A MazF-type mRNA interferase is combined with an antitoxin of unknown fold. Crystals of S. aureus MazF (SaMazF) were grown in space group P2(1)2(1)2(1). The crystals diffracted to 2.1 Å resolution and are likely to contain two SaMazF dim ...[more]

PMID: 21393849

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