2GDC

Structure of Vinculin VD1 / IpaA560-633 complex

Summary for 2GDC

• Entry DOI: 10.2210/pdb2gdc/pdb
• Descriptor: Vinculin, Invasin ipaA (3 entities in total)
• Functional Keywords: ipaa-vinculin complex, shigella flexneri, helical bundle conversion, cell invasion
• Biological source: Gallus gallus (chicken); More
• Cellular location: Cytoplasm, cytoskeleton: P12003; Secreted: P18010
• Total number of polymer chains: 2
• Total formula weight: 31888.02

Authors

Hamiaux, C.,van Eerde, A.,Parsot, C.,Broos, J.,Dijkstra, B.W. (deposition date: 2006-03-15, release date: 2006-08-08, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.74 Å)