Crystallization of the Staphylococcus aureus MazF mRNA interferase.

TitleCrystallization of the Staphylococcus aureus MazF mRNA interferase.
Publication TypeJournal Article
Year of Publication2011
AuthorsZorzini, V., S. Haesaerts, N. P. Donegan, Z. Fu, A. L. Cheung, N. A. J. van Nuland, and R. Loris
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume67
IssuePt 3
Pagination386-9
Date Published2011 Mar 1
Type of Articleta
ISSN1744-3091
KeywordsBacterial Proteins, Crystallization, Crystallography, X-Ray, DNA-Binding Proteins, Endoribonucleases, Molecular Sequence Data, RNA, Messenger, Staphylococcus aureus
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.

DOI10.1107/S1744309111000571
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID21393849
PubMed Central IDPMC3053169
Grant ListAI076298 / AI / NIAID NIH HHS / United States
R01 AI091801 / AI / NIAID NIH HHS / United States
R01 AI091801-02 / AI / NIAID NIH HHS / United States