Open AccessCrystallization of the Staphylococcus aureus MazF mRNA interferase
Author(s) -
Zorzini Valentina,
Haesaerts Sarah,
Donegan Niles P.,
Fu Zhibiao,
Cheung Ambrose L.,
van Nuland Nico A. J.,
Loris Remy
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111000571
Subject(s) - antitoxin , staphylococcus aureus , operon , toxin , messenger rna , microbiology and biotechnology , crystallization , escherichia coli , chemistry , biology , bacteria , gene , biochemistry , genetics , organic chemistry
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 ( Sa MazF) were grown in space group P 2 1 2 1 2 1 . The crystals diffracted to 2.1 Å resolution and are likely to contain two Sa MazF dimers in the asymmetric unit.