View source for 5oh6


==Legionella pneumophila RidL N-terminal domain lacking beta hairpin==
<StructureSection load='5oh6' size='340' side='right'caption='[[5oh6]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5oh6]] is a 2 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=5OH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OH6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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=5oh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oh6 OCA], [https://pdbe.org/5oh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oh6 RCSB], [https://www.ebi.ac.uk/pdbsum/5oh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oh6 ProSAT]</span></td></tr>
</table>
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== 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<ref>PMID:29146912</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5oh6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila subsp. pneumophila ATCC 43290]]
[[Category: Baerlocher K]]
[[Category: Hilbi H]]
[[Category: Hohl M]]
[[Category: Hutter CAJ]]
[[Category: Letourneur F]]
[[Category: Seeger MA]]
[[Category: Steiner B]]
[[Category: Swart AL]]
[[Category: Welin A]]