Title | Crystallization of the Staphylococcus aureus MazF mRNA interferase. |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Zorzini, V., S. Haesaerts, N. P. Donegan, Z. Fu, A. L. Cheung, N. A. J. van Nuland, and R. Loris |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 67 |
Issue | Pt 3 |
Pagination | 386-9 |
Date Published | 2011 Mar 1 |
Type of Article | ta |
ISSN | 1744-3091 |
Keywords | Bacterial 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. |
DOI | 10.1107/S1744309111000571 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 21393849 |
PubMed Central ID | PMC3053169 |
Grant List | AI076298 / AI / NIAID NIH HHS / United States R01 AI091801 / AI / NIAID NIH HHS / United States R01 AI091801-02 / AI / NIAID NIH HHS / United States |
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