4CI6

Mechanisms of crippling actin-dependent phagocytosis by YopO

4CI6 の概要

• エントリーDOI: 10.2210/pdb4ci6/pdb
• 分子名称: ACTIN, PROTEIN KINASE YOPO, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: transferase-structural protein complex, bubonic plague, transferase/structural protein
• 由来する生物種: YERSINIA ENTEROCOLITICA; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114079.75

構造登録者

Lee, W.L.,Grimes, J.M.,Robinson, R.C. (登録日: 2013-12-06, 公開日: 2015-01-28, 最終更新日: 2023-12-20)

主引用文献

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

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: 25664724
DOI: 10.1038/NSMB.2964

実験手法

X-RAY DIFFRACTION (2.651 Å)