Structural highlights
Function
SIDD_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 an adenosine monophosphate-protein hydrolase (de-AMPylase) by mediating the hydrolysis of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby releasing RAB1B from bacterial phagosomes and rendering RAB1B accessible for inactivation by LepB. De-AMPylation of RAB1B cannot take place when LidA is bound to RAB1B.[1] [2] [3]
References
- ↑ Tan Y, Luo ZQ. Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature. 2011 Jul 6;475(7357):506-9. doi: 10.1038/nature10307. PMID:21734656 doi:http://dx.doi.org/10.1038/nature10307
- ↑ Neunuebel MR, Chen Y, Gaspar AH, Backlund PS Jr, Yergey A, Machner MP. De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila. Science. 2011 Jul 22;333(6041):453-6. doi: 10.1126/science.1207193. Epub 2011 Jun, 16. PMID:21680813 doi:http://dx.doi.org/10.1126/science.1207193
- ↑ Neunuebel MR, Mohammadi S, Jarnik M, Machner MP. Legionella pneumophila LidA affects nucleotide binding and activity of the host GTPase Rab1. J Bacteriol. 2012 Mar;194(6):1389-400. doi: 10.1128/JB.06306-11. Epub 2012 Jan 6. PMID:22228731 doi:http://dx.doi.org/10.1128/JB.06306-11
