2GDC

Structure of Vinculin VD1 / IpaA560-633 complex

2GDC の概要

• エントリーDOI: 10.2210/pdb2gdc/pdb
• 分子名称: Vinculin, Invasin ipaA (3 entities in total)
• 機能のキーワード: ipaa-vinculin complex, shigella flexneri, helical bundle conversion, cell invasion
• 由来する生物種: Gallus gallus (chicken); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P12003; Secreted: P18010
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31888.02

構造登録者

Hamiaux, C.,van Eerde, A.,Parsot, C.,Broos, J.,Dijkstra, B.W. (登録日: 2006-03-15, 公開日: 2006-08-08, 最終更新日: 2023-08-30)

主引用文献

Hamiaux, C.,van Eerde, A.,Parsot, C.,Broos, J.,Dijkstra, B.W.
Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri.
Embo Rep., 7:794-799, 2006

PubMed Abstract: Invasion of epithelial cells by Shigella flexneri is characterized by cytoskeletal rearrangements of the host cell membrane, promoting internalization of the bacterium. The bacterial effector IpaA is injected into the epithelial cell by a type III secretion apparatus and recruits vinculin to regulate actin polymerization at the site of entry. We analysed the complex formed between a carboxy-terminal fragment of IpaA (IpaA(560-633)) and the vinculin D1 domain (VD1), both in crystals and in solution. We present evidence that IpaA(560-633) has two alpha-helical vinculin-binding sites that simultaneously bind two VD1 molecules. The interaction of IpaA(560-633) with VD1 is highly similar to the interaction of the endogenous, eukaryotic proteins talin and alpha-actinin with VD1, showing that Shigella uses a structural mimicry strategy to activate vinculin.

PubMed: 16826238
DOI: 10.1038/sj.embor.7400753

実験手法

X-RAY DIFFRACTION (2.74 Å)