5NL1

Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512

Summary for 5NL1

• Entry DOI: 10.2210/pdb5nl1/pdb
• Descriptor: Talin-1, Invasin IpaA, 1,2-ETHANEDIOL, ... (6 entities in total)
• Functional Keywords: structural protein
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 12
• Total formula weight: 127878.36

Authors

Bou-Nader, C.,Pecqueur, L.,Valencia-Gallardo, C.,Fontecave, M.,Tran Van Nhieu, G. (deposition date: 2017-04-03, release date: 2018-05-16, Last modification date: 2024-10-23)

Primary citation

Valencia-Gallardo, C.,Bou-Nader, C.,Aguilar-Salvador, D.I.,Carayol, N.,Quenech'Du, N.,Pecqueur, L.,Park, H.,Fontecave, M.,Izard, T.,Tran Van Nhieu, G.
Shigella IpaA Binding to Talin Stimulates Filopodial Capture and Cell Adhesion.
Cell Rep, 26:921-932.e6, 2019

PubMed Abstract: The Shigella type III effector IpaA contains three binding sites for the focal adhesion protein vinculin (VBSs), which are involved in bacterial invasion of host cells. Here, we report that IpaA VBS3 unexpectedly binds to talin. The 2.5 Å resolution crystal structure of IpaA VBS3 in complex with the talin H1-H4 helices shows a tightly folded α-helical bundle, which is in contrast to the bundle unraveling upon vinculin interaction. High-affinity binding to talin H1-H4 requires a core of hydrophobic residues and electrostatic interactions conserved in talin VBS H46. Remarkably, IpaA VBS3 localizes to filopodial distal adhesions enriched in talin, but not vinculin. In addition, IpaA VBS3 binding to talin was required for filopodial adhesions and efficient capture of Shigella. These results point to the functional diversity of VBSs and support a specific role for talin binding by a subset of VBSs in the formation of filopodial adhesions.

PubMed: 30673614
DOI: 10.1016/j.celrep.2018.12.091

Experimental method

X-RAY DIFFRACTION (2.5 Å)