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| | ==Legionella pneumophila RidL N-terminal retromer binding domain== | | ==Legionella pneumophila RidL N-terminal retromer binding domain== |
| - | <StructureSection load='5oh5' size='340' side='right' caption='[[5oh5]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='5oh5' size='340' side='right'caption='[[5oh5]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oh5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_570-co-h Legionella pneumophila subsp. pneumophila 570-co-h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OH5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oh5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_ATCC_43290 Legionella pneumophila subsp. pneumophila ATCC 43290]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OH5 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lp12_2303 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=933093 Legionella pneumophila subsp. pneumophila 570-CO-H])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=5oh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oh5 OCA], [http://pdbe.org/5oh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oh5 RCSB], [http://www.ebi.ac.uk/pdbsum/5oh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oh5 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oh5 OCA], [https://pdbe.org/5oh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oh5 RCSB], [https://www.ebi.ac.uk/pdbsum/5oh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oh5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Legionella pneumophila subsp. pneumophila 570-co-h]] | + | [[Category: Large Structures]] |
| - | [[Category: Baerlocher, K]] | + | [[Category: Legionella pneumophila subsp. pneumophila ATCC 43290]] |
| - | [[Category: Hilbi, H]] | + | [[Category: Baerlocher K]] |
| - | [[Category: Hohl, M]] | + | [[Category: Hilbi H]] |
| - | [[Category: Hutter, C A.J]] | + | [[Category: Hohl M]] |
| - | [[Category: Letourneur, F]] | + | [[Category: Hutter CAJ]] |
| - | [[Category: Seeger, M A]] | + | [[Category: Letourneur F]] |
| - | [[Category: Steiner, B]] | + | [[Category: Seeger MA]] |
| - | [[Category: Swart, A L]] | + | [[Category: Steiner B]] |
| - | [[Category: Welin, A]] | + | [[Category: Swart AL]] |
| - | [[Category: Novel alpha helical fold]]
| + | [[Category: Welin A]] |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Legionella pneumophila can cause Legionnaires' disease and replicates intracellularly in a distinct Legionella-containing vacuole (LCV). LCV formation is a complex process that involves a plethora of type IV-secreted effector proteins. The effector RidL binds the Vps29 retromer subunit, blocks retrograde vesicle trafficking, and promotes intracellular bacterial replication. Here, we reveal that the 29-kDa N-terminal domain of RidL (RidL2-281) adopts a "foot-like" fold comprising a protruding beta-hairpin at its "heel". The deletion of the beta-hairpin, the exchange to Glu of Ile170 in the beta-hairpin, or Leu152 in Vps29 abolishes the interaction in eukaryotic cells and in vitro. RidL2-281 or RidL displace the Rab7 GTPase-activating protein (GAP) TBC1D5 from the retromer and LCVs, respectively, and TBC1D5 promotes the intracellular growth of L. pneumophila. Thus, the hydrophobic beta-hairpin of RidL is critical for binding of the L. pneumophila effector to the Vps29 retromer subunit and displacement of the regulator TBC1D5.
Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5.,Barlocher K, Hutter CAJ, Swart AL, Steiner B, Welin A, Hohl M, Letourneur F, Seeger MA, Hilbi H Nat Commun. 2017 Nov 16;8(1):1543. doi: 10.1038/s41467-017-01512-5. PMID:29146912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barlocher K, Hutter CAJ, Swart AL, Steiner B, Welin A, Hohl M, Letourneur F, Seeger MA, Hilbi H. Structural insights into Legionella RidL-Vps29 retromer subunit interaction reveal displacement of the regulator TBC1D5. Nat Commun. 2017 Nov 16;8(1):1543. doi: 10.1038/s41467-017-01512-5. PMID:29146912 doi:http://dx.doi.org/10.1038/s41467-017-01512-5
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