5OH5

Legionella pneumophila RidL N-terminal retromer binding domain

Summary for 5OH5

• Entry DOI: 10.2210/pdb5oh5/pdb
• Descriptor: RidL (2 entities in total)
• Functional Keywords: novel alpha helical fold, toxin
• Biological source: Legionella pneumophila subsp. pneumophila ATCC 43290
• Total number of polymer chains: 1
• Total formula weight: 32092.97

Authors

Baerlocher, K.,Hutter, C.A.J.,Swart, A.L.,Steiner, B.,Welin, A.,Hohl, M.,Letourneur, F.,Seeger, M.A.,Hilbi, H. (deposition date: 2017-07-14, release date: 2017-11-22, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)