Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 23, Issue 9, Pages 847-852Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3279
Keywords
-
Funding
- Kimmel Scholar Award from the Sidney Kimmel Foundation for Cancer Research
- University of California Cancer Research Coordination Committee Award [CRC-15-380558]
- March of Dimes Foundation [1-FY15-345]
- US NSF (IOS) [0847870]
- USDA Agriculture Experimental Station Funding [CA-R-PPA-5075-H]
Ask authors/readers for more resources
Effectors secreted by the type Ill secretion system are essential for bacterial pathogenesis. Members of the Yersinia outer-protein J (YopJ) family of effectors found in diverse plant and animal pathogens depend on a protease-like catalytic triad to acetylate host proteins and produce virulence. However, the structural basis for this noncanonical acetyltransferase activity remains unknown. Here, we report the crystal structures of the YopJ effector HopZ1a, produced by the phytopathogen Pseudomonas syringae, in complex with the eukaryote-specific cofactor inositol hexakisphosphate (IP6) and/or coenzyme A (CoA). Structural, computational and functional characterizations reveal a catalytic core with a fold resembling that of ubiquitin-like cysteine proteases and an acetyl-CoA-binding pocket formed after IP6-induced structural rearrangements. Modeling-guided mutagenesis further identified key IP6-interacting residues of Salmonella effector AvrA that are required for acetylating its substrate. Our study reveals the structural basis of a novel class of acetyltransferases and the conserved allosteric regulation of YopJ effectors by IP6.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available