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5oh5

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<StructureSection load='5oh5' size='340' side='right' caption='[[5oh5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5oh5' size='340' side='right' caption='[[5oh5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5oh5]] is a 1 chain structure. 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>
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<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>
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</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>
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</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>
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<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>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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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<div class="pdbe-citations 5oh5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Legionella pneumophila subsp. pneumophila 570-co-h]]
[[Category: Baerlocher, K]]
[[Category: Baerlocher, K]]
[[Category: Hilbi, H]]
[[Category: Hilbi, H]]

Revision as of 07:30, 29 November 2017

Legionella pneumophila RidL N-terminal retromer binding domain

5oh5, resolution 1.90Å

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