View source for 5ot4


==Structure of the Legionella pneumophila effector RidL (1-866)==
<StructureSection load='5ot4' size='340' side='right' caption='[[5ot4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ot4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OT4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5osh|5osh]], [[5osi|5osi]]</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=446 ATCC 33152])</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=5ot4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ot4 OCA], [http://pdbe.org/5ot4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ot4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ot4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ot4 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microbial pathogens employ sophisticated virulence strategies to cause infections in humans. The intracellular pathogen Legionella pneumophila encodes RidL to hijack the host scaffold protein VPS29, a component of retromer and retriever complexes critical for endosomal cargo recycling. Here, we determined the crystal structure of L. pneumophila RidL in complex with the human VPS29-VPS35 retromer subcomplex. A hairpin loop protruding from RidL inserts into a conserved pocket on VPS29 that is also used by cellular ligands, such as Tre-2/Bub2/Cdc16 domain family member 5 (TBC1D5) and VPS9-ankyrin repeat protein for VPS29 binding. Consistent with the idea of molecular mimicry in protein interactions, RidL outcompeted TBC1D5 for binding to VPS29. Furthermore, the interaction of RidL with retromer did not interfere with retromer dimerization but was essential for association of RidL with retromer-coated vacuolar and tubular endosomes. Our work thus provides structural and mechanistic evidence into how RidL is targeted to endosomal membranes.

Molecular mechanism for the subversion of the retromer coat by the Legionella effector RidL.,Romano-Moreno M, Rojas AL, Williamson CD, Gershlick DC, Lucas M, Isupov MN, Bonifacino JS, Machner MP, Hierro A Proc Natl Acad Sci U S A. 2017 Dec 11. pii: 1715361115. doi:, 10.1073/pnas.1715361115. PMID:29229824<ref>PMID:29229824</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ot4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 33152]]
[[Category: Hierro, A]]
[[Category: Isupov, M N]]
[[Category: Lucas, M]]
[[Category: Rojas, A L]]
[[Category: Romano-Moreno, M]]
[[Category: Legionella pneumophila]]
[[Category: Retromer]]
[[Category: Transport protein]]