8C4E

F-actin decorated by SipA426-685

8C4E の概要

• エントリーDOI: 10.2210/pdb8c4e/pdb
• EMDBエントリー: 16425
• 分子名称: Actin, alpha skeletal muscle, Cell invasion protein SipA, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: salmonella invasion, cell invasion
• 由来する生物種: Salmonella; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 454907.03

構造登録者

Yuan, B.,Wald, J.,Marlovits, T.C. (登録日: 2023-01-03, 公開日: 2024-01-17)

主引用文献

Yuan, B.,Scholz, J.,Wald, J.,Thuenauer, R.,Hennell James, R.,Ellenberg, I.,Windhorst, S.,Faix, J.,Marlovits, T.C.
Structural basis for subversion of host cell actin cytoskeleton during Salmonella infection.
Sci Adv, 9:eadj5777-eadj5777, 2023

PubMed Abstract: Secreted bacterial type III secretion system (T3SS) proteins are essential for successful infection by many human pathogens. Both T3SS translocator SipC and effector SipA are critical for infection by subversion of the host cell cytoskeleton, but the precise molecular interplay between them remains unknown. Here, using cryo-electron microscopy, we show that SipA binds along the F-actin grooves with a unique binding pattern. SipA stabilizes F-actin through charged interface residues and appears to prevent inorganic phosphate release through closure of the "back door" of adenosine 5'-triphosphate pocket. We also show that SipC enhances the binding of SipA to F-actin, thus demonstrating that a sequential presence of T3SS proteins in host cells is associated with a sequence of infection events-starting with actin nucleation, filament growth, and stabilization. Together, our data explain the coordinated interplay of a precisely tuned and highly effective mechanism during infection and provide a blueprint for interfering with effectors acting on actin.

PubMed: 38064550
DOI: 10.1126/sciadv.adj5777

実験手法

ELECTRON MICROSCOPY (2.6 Å)