View source for 4pay


==Crystal structure of an N-terminal fragment of the Legionella pneumophila effector protein SidC.==
<StructureSection load='4pay' size='340' side='right'caption='[[4pay]], [[Resolution|resolution]] 2.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pay]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4om6 4om6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PAY 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]] 2.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4pay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pay OCA], [https://pdbe.org/4pay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pay RCSB], [https://www.ebi.ac.uk/pdbsum/4pay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pay ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5ZSK6_LEGPH Q5ZSK6_LEGPH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tethering proteins play a key role in vesicular transport, ensuring that cargo arrives at a specific destination. The bacterial effector protein SidC and its paralog SdcA have been described as tethering factors encoded by the intracellular pathogen Legionella pneumophila. Here, we demonstrate that SidC proteins are important for early events unique to maturation of vacuoles containing Legionella and discover monoubiquitination of Rab1 as a new SidC-dependent activity. The crystal structure of the SidC N-terminus revealed a novel fold that is important for function and could be involved in Legionella adaptations to evolutionarily divergent host cells it encounters in natural environments.

Legionella pneumophila Subversion of Host Vesicular Transport by SidC Effector Proteins.,Horenkamp FA, Mukherjee S, Alix E, Schauder CM, Hubber AM, Roy CR, Reinisch KM Traffic. 2014 May;15(5):488-99. doi: 10.1111/tra.12158. Epub 2014 Mar 12. PMID:24483784<ref>PMID:24483784</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pay" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
[[Category: Alix E]]
[[Category: Horenkamp FA]]
[[Category: Hubber AM]]
[[Category: Mukherjee S]]
[[Category: Reinisch KM]]
[[Category: Roy CR]]
[[Category: Schauder CM]]