5oh6 | pdb_00005oh6

Legionella pneumophila RidL N-terminal domain lacking beta hairpin

spinqualitylabelsall models 5oh6, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5oh6 is a 2 chain structure with sequence from Legionella pneumophila subsp. pneumophila ATCC 43290. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 (RidL2-281) adopts a "foot-like" fold comprising a protruding beta-hairpin at its "heel". The deletion of the beta-hairpin, the exchange to Glu of Ile170 in the beta-hairpin, or Leu152 in Vps29 abolishes the interaction in eukaryotic cells and in vitro. RidL2-281 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 beta-hairpin of RidL is critical for binding of the L. pneumophila effector to the Vps29 retromer subunit and displacement of the regulator TBC1D5. Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5.,Barlocher K, Hutter CAJ, Swart AL, Steiner B, Welin A, Hohl M, Letourneur F, Seeger MA, Hilbi H Nat Commun. 2017 Nov 16;8(1):1543. doi: 10.1038/s41467-017-01512-5. PMID:29146912 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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