Structural highlights
Function
RAB1B_HUMAN Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments.[1]
Publication Abstract from PubMed
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.
Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB.,Mihai Gazdag E, Streller A, Haneburger I, Hilbi H, Vetter IR, Goody RS, Itzen A EMBO Rep. 2013 Jan 4. doi: 10.1038/embor.2012.211. PMID:23288104[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Overmeyer JH, Wilson AL, Erdman RA, Maltese WA. The putative "switch 2" domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein. Mol Biol Cell. 1998 Jan;9(1):223-35. PMID:9437002
- ↑ Mihai Gazdag E, Streller A, Haneburger I, Hilbi H, Vetter IR, Goody RS, Itzen A. Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. EMBO Rep. 2013 Jan 4. doi: 10.1038/embor.2012.211. PMID:23288104 doi:http://dx.doi.org/10.1038/embor.2012.211
