4CI6
Mechanisms of crippling actin-dependent phagocytosis by YopO
Summary for 4CI6
| Entry DOI | 10.2210/pdb4ci6/pdb |
| Descriptor | ACTIN, PROTEIN KINASE YOPO, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | transferase-structural protein complex, bubonic plague, transferase/structural protein |
| Biological source | YERSINIA ENTEROCOLITICA More |
| Total number of polymer chains | 2 |
| Total formula weight | 114079.75 |
| Authors | Lee, W.L.,Grimes, J.M.,Robinson, R.C. (deposition date: 2013-12-06, release date: 2015-01-28, Last modification date: 2023-12-20) |
| Primary citation | Lee, W.L.,Grimes, J.M.,Robinson, R.C. Yersinia Effector Yopo Uses Actin as Bait to Phosphorylate Proteins that Regulate Actin Polymerization. Nat.Struct.Mol.Biol., 22:248-, 2015 Cited by PubMed Abstract: 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 biochemical analyses confirm that actin-polymerization regulators such as VASP, EVL, WASP, gelsolin and the formin diaphanous 1 are directly sequestered and phosphorylated by YopO through formation of ternary complexes with actin. This leads to a model in which YopO at the membrane sequesters actin from polymerization while using the bound actin as bait to recruit, phosphorylate and misregulate host actin-regulating proteins to disrupt phagocytosis. PubMed: 25664724DOI: 10.1038/NSMB.2964 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.651 Å) |
Structure validation
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