The Bacterial Effector VopL Organizes Actin into Filament-like Structures

@article{Zahm2013TheBE,
  title={The Bacterial Effector VopL Organizes Actin into Filament-like Structures},
  author={Jacob A. Zahm and Shae B. Padrick and Zhucheng Chen and Chi W. Pak and Ali A. Yunus and Lisa M Henry and Diana R Tomchick and Zhe Chen and Michael K Rosen},
  journal={Cell},
  year={2013},
  volume={155},
  pages={423-434}
}
VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal domain (VCD) and an array of three WASP homology 2 (WH2) motifs. Here, we report the crystal structure of the VCD dimer bound to actin. The VCD organizes three actin monomers in a spatial arrangement close to that found in the canonical actin filament. In this arrangement, WH2 motifs can be modeled into the binding site of each actin without steric clashes. The data… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 1 time. VIEW TWEETS

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

Actin filament assembly by bacterial factors VopL/F: Which end is up?

The Journal of cell biology • 2017
View 14 Excerpts
Highly Influenced

Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells.

Proceedings of the National Academy of Sciences of the United States of America • 2015

References

Publications referenced by this paper.
Showing 1-10 of 57 references

The structural basis of actin filament branching by the Arp2/3 complex

The Journal of cell biology • 2008
View 6 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…