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5NL1

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

5NL1 の概要
エントリーDOI10.2210/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: 30673614
DOI: 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)
構造検証レポート
Validation report summary of 5nl1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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