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5o74
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human Rab1b covalently bound to the GEF domain of DrrA/SidM from Legionella pneumophila in the presence of GDP== | |
| + | <StructureSection load='5o74' size='340' side='right' caption='[[5o74]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5o74]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O74 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=9MN:'>9MN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5o74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o74 OCA], [http://pdbe.org/5o74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o74 RCSB], [http://www.ebi.ac.uk/pdbsum/5o74 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o74 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DRRA_LEGPN DRRA_LEGPN]] 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:16906144</ref> <ref>PMID:17952054</ref> <ref>PMID:20651120</ref> [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The characterization of low-affinity protein complexes is challenging due to their dynamic nature. Here we present a method to stabilize transient protein complexes in vivo by generating a covalent and conformationally flexible bridge between the interaction partners. A highly active pyrrolysyl tRNA synthetase mutant directs the incorporation of unnatural amino acids bearing bromoalkyl moieties (BrCnK) into proteins. We demonstrate for the first time that low-affinity protein complexes between BrCnK-containing proteins and their binding partners can be stabilized in vivo in bacterial and mammalian cells. Using this approach we determined the crystal structure of a transient GDP-bound complex between a small G-protein and its nucleotide exchange factor. We envision that this approach will prove valuable as a general tool for validating and characterizing protein-protein interactions in vitro and in vivo. | ||
| - | + | Proximity-triggered covalent stabilization of low-affinity protein complexes in vitro and in vivo.,Cigler M, Muller TG, Horn-Ghetko D, von Wrisberg MK, Fottner M, Goody RS, Itzen A, Muller MP, Lang K Angew Chem Int Ed Engl. 2017 Sep 28. doi: 10.1002/anie.201706927. PMID:28960788<ref>PMID:28960788</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5o74" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Cigler, M]] | ||
[[Category: Fottner, M]] | [[Category: Fottner, M]] | ||
| - | [[Category: | + | [[Category: Goody, R S]] |
[[Category: Horn-Ghetko, D]] | [[Category: Horn-Ghetko, D]] | ||
| + | [[Category: Itzen, A]] | ||
[[Category: Lang, K]] | [[Category: Lang, K]] | ||
| - | [[Category: | + | [[Category: Mueller, M P]] |
| + | [[Category: Mueller, T]] | ||
| + | [[Category: Wrisberg, M K.von]] | ||
| + | [[Category: Drra]] | ||
| + | [[Category: Exchange factor]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Legionella pneumophila]] | ||
| + | [[Category: Rab1b]] | ||
Revision as of 06:51, 11 October 2017
Crystal structure of human Rab1b covalently bound to the GEF domain of DrrA/SidM from Legionella pneumophila in the presence of GDP
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Categories: Cigler, M | Fottner, M | Goody, R S | Horn-Ghetko, D | Itzen, A | Lang, K | Mueller, M P | Mueller, T | Wrisberg, M K.von | Drra | Exchange factor | Hydrolase | Legionella pneumophila | Rab1b
