Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization

@article{Lee2015YersiniaEY,
  title={Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization},
  author={Wei Lin Lee and Jonathan M Grimes and Robert C Robinson},
  journal={Nature Structural &Molecular Biology},
  year={2015},
  volume={22},
  pages={248-255}
}
Pathogenic Yersinia species evade host immune systems through the injection of Yersinia outer proteins (Yops) into phagocytic cells. One Yop, YopO, also known as YpkA, induces actin-filament disruption, impairing phagocytosis. Here we describe the X-ray structure of Yersinia enterocolitica YopO in complex with actin, which reveals that YopO binds to an actin monomer in a manner that blocks polymerization yet allows the bound actin to interact with host actin-regulating proteins. SILAC-MS and… CONTINUE READING
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References

Publications referenced by this paper.
Showing 1-10 of 60 references

Decision making in xia2

Acta crystallographica. Section D, Biological crystallography • 2013

Guardians of the actin monomer.

European journal of cell biology • 2013

How good are my data and what is the resolution?

Acta crystallographica. Section D, Biological crystallography • 2013

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