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4iik

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Revision as of 16:04, 19 June 2013 by OCA (Talk | contribs)
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Template:STRUCTURE 4iik

Contents

Legionella pneumophila effector

Template:ABSTRACT PUBMED 23696742

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]

About this Structure

4iik is a 1 chain structure with sequence from Legionella pneumophila subsp. pneumophila str. philadelphia 1. Full crystallographic information is available from OCA.

Reference

  • Chen Y, Tascon I, Neunuebel MR, Pallara C, Brady J, Kinch LN, Fernandez-Recio J, Rojas AL, Machner MP, Hierro A. Structural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidD. PLoS Pathog. 2013 May;9(5):e1003382. doi: 10.1371/journal.ppat.1003382. Epub 2013, May 16. PMID:23696742 doi:10.1371/journal.ppat.1003382
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

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