Structural highlights
Function
LEM3_LEGPH Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a phosphocholine hydrolase by mediating the hydrolysis of phosphocholine to Ser residues of host RAB1 (RAB1A, RAB1B or RAB1C). Dephosphocholination of target proteins restores accessibility to GTPase effector LepB. Can act on both GDP-bound and GTP-bound Rab proteins.[1] [2] [3]
References
- ↑ Tan Y, Arnold RJ, Luo ZQ. Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):21212-7. doi:, 10.1073/pnas.1114023109. Epub 2011 Dec 7. PMID:22158903 doi:10.1073/pnas.1114023109
- ↑ Goody PR, Heller K, Oesterlin LK, Muller MP, Itzen A, Goody RS. Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. EMBO J. 2012 Feb 3;31(7):1774-84. doi: 10.1038/emboj.2012.16. PMID:22307087 doi:10.1038/emboj.2012.16
- ↑ Oesterlin LK, Goody RS, Itzen A. Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor. Proc Natl Acad Sci U S A. 2012 Apr 10;109(15):5621-6. doi:, 10.1073/pnas.1121161109. Epub 2012 Mar 12. PMID:22411835 doi:10.1073/pnas.1121161109
