View source for 2wzg


==Legionella glucosyltransferase (Lgt1) crystal structure==
<StructureSection load='2wzg' size='340' side='right'caption='[[2wzg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wzg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WZG 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</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=2wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wzg OCA], [https://pdbe.org/2wzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wzg RCSB], [https://www.ebi.ac.uk/pdbsum/2wzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wzg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5WWY0_LEGPL Q5WWY0_LEGPL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Legionnaires' disease is caused by a lethal colonization of alveolar macrophages with the Gram-negative bacterium Legionella pneumophila. LpGT (L. pneumophila glucosyltransferase; also known as Lgt1) has recently been identified as a virulence factor, shutting down protein synthesis in the human cell by specific glucosylation of EF1A (elongation factor 1A), using an unknown mode of substrate recognition and a retaining mechanism for glycosyl transfer. We have determined the crystal structure of LpGT in complex with substrates, revealing a GT-A fold with two unusual protruding domains. Through structure-guided mutagenesis of LpGT, several residues essential for binding of the UDP-glucose-donor and EF1A-acceptor substrates were identified, which also affected L. pneumophila virulence as demonstrated by microinjection studies. Together, these results suggested that a positively charged EF1A loop binds to a negatively charged conserved groove on the LpGT structure, and that two asparagine residues are essential for catalysis. Furthermore, we showed that two further L. pneumophila glycosyltransferases possessed the conserved UDP-glucose-binding sites and EF1A-binding grooves, and are, like LpGT, translocated into the macrophage through the Icm/Dot (intracellular multiplication/defect in organelle trafficking) system.

Molecular mechanism of elongation factor 1A inhibition by a Legionella pneumophila glycosyltransferase.,Hurtado-Guerrero R, Zusman T, Pathak S, Ibrahim AF, Shepherd S, Prescott A, Segal G, van Aalten DM Biochem J. 2010 Feb 24;426(3):281-92. PMID:20030628<ref>PMID:20030628</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2wzg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila]]
[[Category: Hurtado-Guerrero R]]
[[Category: Ibrahim AFM]]
[[Category: Pathak S]]
[[Category: Prescott A]]
[[Category: Segal G]]
[[Category: Shepherd S]]
[[Category: Van Aalten DMF]]
[[Category: Zusman T]]