5OH6

Legionella pneumophila RidL N-terminal domain lacking beta hairpin

5OH6 の概要

• エントリーDOI: 10.2210/pdb5oh6/pdb
• 分子名称: Interaptin (2 entities in total)
• 機能のキーワード: novel alpha helical fold, toxin
• 由来する生物種: Legionella pneumophila subsp. pneumophila ATCC 43290
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53189.37

構造登録者

Baerlocher, K.,Hutter, C.A.J.,Swart, A.L.,Steiner, B.,Welin, A.,Hohl, M.,Letourneur, F.,Seeger, M.A.,Hilbi, H. (登録日: 2017-07-14, 公開日: 2017-11-22, 最終更新日: 2024-05-08)

主引用文献

Barlocher, K.,Hutter, C.A.J.,Swart, A.L.,Steiner, B.,Welin, A.,Hohl, M.,Letourneur, F.,Seeger, M.A.,Hilbi, H.
Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5.
Nat Commun, 8:1543-1543, 2017

PubMed Abstract: Legionella pneumophila can cause Legionnaires' disease and replicates intracellularly in a distinct Legionella-containing vacuole (LCV). LCV formation is a complex process that involves a plethora of type IV-secreted effector proteins. The effector RidL binds the Vps29 retromer subunit, blocks retrograde vesicle trafficking, and promotes intracellular bacterial replication. Here, we reveal that the 29-kDa N-terminal domain of RidL (RidL) adopts a "foot-like" fold comprising a protruding β-hairpin at its "heel". The deletion of the β-hairpin, the exchange to Glu of Ile in the β-hairpin, or Leu in Vps29 abolishes the interaction in eukaryotic cells and in vitro. RidL or RidL displace the Rab7 GTPase-activating protein (GAP) TBC1D5 from the retromer and LCVs, respectively, and TBC1D5 promotes the intracellular growth of L. pneumophila. Thus, the hydrophobic β-hairpin of RidL is critical for binding of the L. pneumophila effector to the Vps29 retromer subunit and displacement of the regulator TBC1D5.

PubMed: 29146912
DOI: 10.1038/s41467-017-01512-5

実験手法

X-RAY DIFFRACTION (2.05 Å)