This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4iip
From Proteopedia
| Line 1: | Line 1: | ||
| - | + | {{STRUCTURE_4iip| PDB=4iip | SCENE= }} | |
| + | ===Legionella pneumophila effector=== | ||
| + | {{ABSTRACT_PUBMED_23696742}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/SIDD_LEGPH 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.<ref>PMID:21734656</ref> <ref>PMID:21680813</ref> <ref>PMID:22228731</ref> | ||
| - | + | ==About this Structure== | |
| + | [[4iip]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._philadelphia_1 Legionella pneumophila subsp. pneumophila str. philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IIP OCA]. | ||
| - | + | ==Reference== | |
| + | <ref group="xtra">PMID:023696742</ref><references group="xtra"/><references/> | ||
| + | [[Category: Legionella pneumophila subsp. pneumophila str. philadelphia 1]] | ||
| + | [[Category: Chen, Y.]] | ||
| + | [[Category: Hierro, A.]] | ||
| + | [[Category: Machner, M P.]] | ||
| + | [[Category: Neunuebel, M R.]] | ||
| + | [[Category: Rojas, A L.]] | ||
| + | [[Category: Tascon, I.]] | ||
| + | [[Category: Beta sandwich]] | ||
| + | [[Category: De-ampylation]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Legionella containing vacuole surface]] | ||
| + | [[Category: Rab1]] | ||
Revision as of 15:59, 19 June 2013
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
4iip 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
- ↑ 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
