Structure and function of Fic proteins
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Immunology and Microbiology,Microbiology,Infectious Diseases
Link
http://www.nature.com/articles/nrmicro3520.pdf
Reference54 articles.
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2. Garcia-Pino, A. et al. Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. J. Biol. Chem. 283, 30821–30827 (2008).
3. Arbing, M. A. et al. Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure 18, 996–1010 (2010).
4. Engel, P. et al. Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins. Nature 482, 107–110 (2012). This study uncovers a mechanism of inhibition common to the VbhA–VbhT toxin–antitoxin module and Fic toxins, which involves the insertion of an inhibitory glutamate into the FIC active site.
5. Lee, C. C. et al. Crystal structure of the type III effector AvrB from Pseudomonas syringae. Structure 12, 487–494 (2004).
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