3jza
From Proteopedia
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{{STRUCTURE_3jza| PDB=3jza | SCENE= }} | {{STRUCTURE_3jza| PDB=3jza | SCENE= }} | ||
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===Crystal structure of human Rab1b in complex with the GEF domain of DrrA/SidM from Legionella pneumophila=== | ===Crystal structure of human Rab1b in complex with the GEF domain of DrrA/SidM from Legionella pneumophila=== | ||
| + | {{ABSTRACT_PUBMED_20064470}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/RAB1B_HUMAN RAB1B_HUMAN]] Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments.<ref>PMID:9437002</ref> [[http://www.uniprot.org/uniprot/Q5ZSQ3_LEGPH Q5ZSQ3_LEGPH]] Virulence effector that plays a key 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 GDP-GTP exchange factor (GEF) for the small GTPase Rab1 (RAB1A, RAB1B or RAB1C), thereby converting Rab1 to an active GTP-bound state, leading to the incorporation of Rab1 into LCVs. Also shows RabGDI displacement factor (GDF) activity; however, this probably represents a passive activity following the GEF activity. Also acts as an adenylyltransferase by mediating the addition of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby rendering RAB1B constitutively active. Also has adenylyltransferase activity towards Rab6 and Rab35. Also displays guanylyltransferase activity by mediating the addition of guanosine 5'-monophosphate (GMP) to host RAB1B in vitro; however such activity remains uncertain in vivo. Specifically binds phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection.<ref>PMID:16824952</ref><ref>PMID:17947549</ref><ref>PMID:21822290</ref><ref>PMID:20064470</ref><ref>PMID:19942850</ref><ref>PMID:20176951</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020064470</ref><ref group="xtra">PMID:017947549</ref><ref group="xtra">PMID:017952054</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Legionella pneumophila subsp. pneumophila str. philadelphia 1]] | [[Category: Legionella pneumophila subsp. pneumophila str. philadelphia 1]] | ||
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[[Category: Oesterlin, L K.]] | [[Category: Oesterlin, L K.]] | ||
[[Category: Schoebel, S.]] | [[Category: Schoebel, S.]] | ||
| - | [[Category: Acetylation]] | ||
| - | [[Category: Cytoplasm]] | ||
[[Category: Gdf]] | [[Category: Gdf]] | ||
[[Category: Gdi]] | [[Category: Gdi]] | ||
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[[Category: Rabgdi]] | [[Category: Rabgdi]] | ||
[[Category: Rabgef]] | [[Category: Rabgef]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 09:44, 27 March 2013
Contents |
Crystal structure of human Rab1b in complex with the GEF domain of DrrA/SidM from Legionella pneumophila
Template:ABSTRACT PUBMED 20064470
Function
[RAB1B_HUMAN] Protein transport. Regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments.[1] [Q5ZSQ3_LEGPH] Virulence effector that plays a key 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 GDP-GTP exchange factor (GEF) for the small GTPase Rab1 (RAB1A, RAB1B or RAB1C), thereby converting Rab1 to an active GTP-bound state, leading to the incorporation of Rab1 into LCVs. Also shows RabGDI displacement factor (GDF) activity; however, this probably represents a passive activity following the GEF activity. Also acts as an adenylyltransferase by mediating the addition of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby rendering RAB1B constitutively active. Also has adenylyltransferase activity towards Rab6 and Rab35. Also displays guanylyltransferase activity by mediating the addition of guanosine 5'-monophosphate (GMP) to host RAB1B in vitro; however such activity remains uncertain in vivo. Specifically binds phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection.[2][3][4][5][6][7]
About this Structure
3jza is a 2 chain structure with sequence from Homo sapiens and Legionella pneumophila subsp. pneumophila str. philadelphia 1. Full crystallographic information is available from OCA.
Reference
- Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol Cell. 2009 Dec 25;36(6):1060-72. PMID:20064470 doi:10.1016/j.molcel.2009.11.014
- Machner MP, Isberg RR. A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science. 2007 Nov 9;318(5852):974-7. Epub 2007 Oct 18. PMID:17947549
- Ingmundson A, Delprato A, Lambright DG, Roy CR. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature. 2007 Nov 15;450(7168):365-9. Epub 2007 Oct 21. PMID:17952054 doi:10.1038/nature06336
- ↑ 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
- ↑ Machner MP, Isberg RR. Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev Cell. 2006 Jul;11(1):47-56. PMID:16824952 doi:10.1016/j.devcel.2006.05.013
- ↑ Machner MP, Isberg RR. A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science. 2007 Nov 9;318(5852):974-7. Epub 2007 Oct 18. PMID:17947549
- ↑ Mukherjee S, Liu X, Arasaki K, McDonough J, Galan JE, Roy CR. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature. 2011 Aug 7;477(7362):103-6. doi: 10.1038/nature10335. PMID:21822290 doi:10.1038/nature10335
- ↑ Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol Cell. 2009 Dec 25;36(6):1060-72. PMID:20064470 doi:10.1016/j.molcel.2009.11.014
- ↑ Suh HY, Lee DW, Lee KH, Ku B, Choi SJ, Woo JS, Kim YG, Oh BH. Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA. EMBO J. 2010 Jan 20;29(2):496-504. Epub 2009 Nov 26. PMID:19942850 doi:10.1038/emboj.2009.347
- ↑ Zhu Y, Hu L, Zhou Y, Yao Q, Liu L, Shao F. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proc Natl Acad Sci U S A. 2010 Mar 9;107(10):4699-704. Epub 2010 Feb 22. PMID:20176951 doi:10.1073/pnas.0914231107
Categories: Homo sapiens | Legionella pneumophila subsp. pneumophila str. philadelphia 1 | Blankenfeldt, W. | Goody, R S. | Itzen, A. | Oesterlin, L K. | Schoebel, S. | Gdf | Gdi | Gdi displacement factor | Gef | Gtp-binding | Lipoprotein | Membrane | Nucleotide-binding | Prenylation | Protein transport | Rabgdi | Rabgef | Transport protein
