4ci6 | pdb_00004ci6

Mechanisms of crippling actin-dependent phagocytosis by YopO

spinqualitylabelsall models 4ci6, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ci6 is a 2 chain structure with sequence from [1] and Spodoptera frugiperda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, CA Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization.,Lee WL, Grimes JM, Robinson RC Nat Struct Mol Biol. 2015 Feb 9. doi: 10.1038/nsmb.2964. PMID:25664724 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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