View source for 8jo4


==Cryo-EM structure of a Legionella effector complexed with actin and ATP==
<StructureSection load='8jo4' size='340' side='right'caption='[[8jo4]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8jo4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_sainthelensi Legionella sainthelensi] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JO4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.04&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8jo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jo4 OCA], [https://pdbe.org/8jo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jo4 RCSB], [https://www.ebi.ac.uk/pdbsum/8jo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jo4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2H5FI52_9GAMM A0A2H5FI52_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
AMPylation is a post-translational modification in which AMP is added to the amino acid side chains of proteins(1,2). Here we show that, with ATP as the ligand and actin as the host activator, the effector protein LnaB of Legionella pneumophila exhibits AMPylase activity towards the phosphoryl group of phosphoribose on PR(R42)-Ub that is generated by the SidE family of effectors, and deubiquitinases DupA and DupB in an E1- and E2-independent ubiquitination process(3-7). The product of LnaB is further hydrolysed by an ADP-ribosylhydrolase, MavL, to Ub, thereby preventing the accumulation of PR(R42)-Ub and ADPR(R42)-Ub and protecting canonical ubiquitination in host cells. LnaB represents a large family of AMPylases that adopt a common structural fold, distinct from those of the previously known AMPylases, and LnaB homologues are found in more than 20 species of bacterial pathogens. Moreover, LnaB also exhibits robust phosphoryl AMPylase activity towards phosphorylated residues and produces unique ADPylation modifications in proteins. During infection, LnaB AMPylates the conserved phosphorylated tyrosine residues in the activation loop of the Src family of kinases(8,9), which dampens downstream phosphorylation signalling in the host. Structural studies reveal the actin-dependent activation and catalytic mechanisms of the LnaB family of AMPylases. This study identifies, to our knowledge, an unprecedented molecular regulation mechanism in bacterial pathogenesis and protein phosphorylation.

Legionella effector LnaB is a phosphoryl AMPylase that impairs phosphosignalling.,Wang T, Song X, Tan J, Xian W, Zhou X, Yu M, Wang X, Xu Y, Wu T, Yuan K, Ran Y, Yang B, Fan G, Liu X, Zhou Y, Zhu Y Nature. 2024 May 22. doi: 10.1038/s41586-024-07573-z. PMID:38776962<ref>PMID:38776962</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8jo4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella sainthelensi]]
[[Category: Oryctolagus cuniculus]]
[[Category: Tan JX]]
[[Category: Wang XF]]
[[Category: Zhou XT]]
[[Category: Zhu YQ]]