2gdc | pdb_00002gdc
Structure of Vinculin VD1 / IpaA560-633 complex
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Overview
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.
About this Structure
2GDC is a Protein complex structure of sequences from Gallus gallus and Shigella flexneri. Full crystallographic information is available from OCA.
Reference
Structural mimicry for vinculin activation by IpaA, a virulence factor of Shigella flexneri., Hamiaux C, van Eerde A, Parsot C, Broos J, Dijkstra BW, EMBO Rep. 2006 Aug;7(8):794-9. Epub 2006 Jul 7. PMID:16826238
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