5NL1
Shigella IpaA-VBS3/TBS in complex with the Talin VBS1 domain 488-512
5NL1 の概要
| エントリーDOI | 10.2210/pdb5nl1/pdb |
| 分子名称 | Talin-1, Invasin IpaA, 1,2-ETHANEDIOL, ... (6 entities in total) |
| 機能のキーワード | structural protein |
| 由来する生物種 | Mus musculus (Mouse) 詳細 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 127878.36 |
| 構造登録者 | Bou-Nader, C.,Pecqueur, L.,Valencia-Gallardo, C.,Fontecave, M.,Tran Van Nhieu, G. (登録日: 2017-04-03, 公開日: 2018-05-16, 最終更新日: 2024-10-23) |
| 主引用文献 | 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 Cited by 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: 30673614DOI: 10.1016/j.celrep.2018.12.091 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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