Journal
EMBO REPORTS
Volume 14, Issue 2, Pages 199-205Publisher
WILEY
DOI: 10.1038/embor.2012.211
Keywords
vesicular trafficking; Legionnaires' disease GTPase; pathogen vacuole
Categories
Funding
- Max-Planck-Society
- DFG [SPP1580, HI 1511/3-1]
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Legionella pneumophila is an intracellularly surviving pathogen that releases about 270 different proteins into the host cell during infection. A set of secreted proteins takes control of the vesicular trafficking regulator Rab1. Legionella LepB inactivates Rab1 by acting as a GTPase-activating protein (GAP). We present the crystal structure of the Rab1b:LepB complex together with a thorough biochemical analysis and show that the GAP domain of LepB consists of an unusual fold. LepB acts by an atypical RabGAP mechanism that is reminiscent of classical GAPs and therefore sets the protein apart from mammalian TBC-like GAPs. Surprisingly, LepB can function as a GAP for Rab3, Rab8, Rab13 and Rab35, too, suggesting that it has a broader cellular role than previously thought.
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