3jz9

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'''Unreleased structure'''
 
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The entry 3jz9 is ON HOLD until Paper Publication
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==Crystal structure of the GEF domain of DrrA/SidM from Legionella pneumophila==
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<StructureSection load='3jz9' size='340' side='right'caption='[[3jz9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3jz9]] is a 1 chain structure with sequence from [https://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=3JZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JZ9 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3jz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jz9 OCA], [https://pdbe.org/3jz9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jz9 RCSB], [https://www.ebi.ac.uk/pdbsum/3jz9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jz9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DRRA_LEGPH DRRA_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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Prenylated Rab proteins exist in the cytosol as soluble, high-affinity complexes with GDI that need to be disrupted for membrane attachment and targeting of Rab proteins. The Legionella pneumophila protein DrrA displaces GDI from Rab1:GDI complexes, incorporating Rab1 into Legionella-containing vacuoles and activating Rab1 by exchanging GDP for GTP. Here, we present the crystal structure of a complex between the GEF domain of DrrA and Rab1 and a detailed kinetic analysis of this exchange. DrrA efficiently catalyzes nucleotide exchange and mimics the general nucleotide exchange mechanism of mammalian GEFs for Ras-like GTPases. We show that the GEF activity of DrrA is sufficient to displace prenylated Rab1 from the Rab1:GDI complex. Thus, apparent GDI displacement by DrrA is linked directly to nucleotide exchange, suggesting a basic model for GDI displacement and specificity of Rab localization that does not require discrete GDI displacement activity.
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Authors: Schoebel, S., Oesterlin, L.K., Blankenfeldt, W., Goody, R.S., Itzen, A.
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RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity.,Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A Mol Cell. 2009 Dec 25;36(6):1060-72. PMID:20064470<ref>PMID:20064470</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 21 10:00:02 2009''
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<div class="pdbe-citations 3jz9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
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[[Category: Blankenfeldt W]]
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[[Category: Goody RS]]
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[[Category: Itzen A]]
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[[Category: Oesterlin LK]]
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[[Category: Schoebel S]]

Current revision

Crystal structure of the GEF domain of DrrA/SidM from Legionella pneumophila

PDB ID 3jz9

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