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6s5t

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'''Unreleased structure'''
 
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The entry 6s5t is ON HOLD until Paper Publication
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==Legionella pneumophila SidJ-Human calmodulin complex==
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<SX load='6s5t' size='340' side='right' viewer='molstar' caption='[[6s5t]], [[Resolution|resolution]] 4.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6s5t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S5T FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6s5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s5t OCA], [https://pdbe.org/6s5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s5t RCSB], [https://www.ebi.ac.uk/pdbsum/6s5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s5t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SIDJ_LEGPH SIDJ_LEGPH] Glutamylase that mediates the covalent attachment of glutamate moieties to SdeA on one of the catalytic residues that is required for its mono-ADP-ribosyltransferase activity (PubMed:31330532, PubMed:31330531). In turn, inhibits SdeA ubiquitinating activity. Glutamylates also related SdeB, SdeC and SidE (PubMed:31330531, PubMed:31123136). Glutamylase activity only occurs in the host since it requires host calmodulin (PubMed:28497808, PubMed:31330532, PubMed:31330531, PubMed:31123136). May also reverse the SdeA-mediated substrate ubiquitination by cleaving the phosphodiester bond that links phosphoribosylated ubiquitin to protein substrates via its deubiquitinase activity (PubMed:28497808).<ref>PMID:28497808</ref> <ref>PMID:31123136</ref> <ref>PMID:31330531</ref> <ref>PMID:31330532</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The family of bacterial SidE enzymes catalyses phosphoribosyl-linked (PR) serine ubiquitination and promotes infectivity of Legionella pneumophilia, a pathogenic bacterium causing Legionnaires' disease(1-3). SidEs share the genetic locus with the Legionella effector SidJ that spatiotemporally opposes their toxicity in yeast and mammalian cells, through an unknown mechanism(4-6). Deletion of SidJ leads to a significant defect in the growth of Legionella in both its natural host amoeba and in murine macrophages(4,5). Here, we demonstrate that SidJ is a glutamylase that modifies the catalytic glutamate in the mono-ADPribosyl transferase (mART) domain of SdeA thus blocking its ubiquitin (Ub) ligase activity. SidJ glutamylation activity requires interaction with calmodulin (CaM), a eukaryotic specific co-factor, and can be regulated by intracellular changes in Ca(2+) concentrations. The cryo-EM structure of SidJ/human apo-CaM complex revealed the architecture of this unique heterodimeric glutamylase. In infected cells, we show that SidJ mediates glutamylation of SidEs on the surface of Legionella-containing vacuoles (LCVs). Using quantitative proteomics, we also uncovered multiple host proteins as putative targets of SidJ-mediated glutamylation. Collectively, this study reveals the mechanism of SidE ligases inhibition by a SidJ/CaM glutamylase and opens new avenues for studying protein glutamylation, an understudied protein modification in higher eukaryotes.
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Authors: Bhogaraju, S., Galej, W.P., Pfleiderer, M.M., Adams, M.
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Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin-catalysed glutamylation.,Bhogaraju S, Bonn F, Mukherjee R, Adams M, Pfleiderer MM, Galej WP, Matkovic V, Lopez-Mosqueda J, Kalayil S, Shin D, Dikic I Nature. 2019 Jul 22. pii: 10.1038/s41586-019-1440-8. doi:, 10.1038/s41586-019-1440-8. PMID:31330532<ref>PMID:31330532</ref>
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Description: Legionella pneumophila SidJ-Human calmodulin complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Adams, M]]
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<div class="pdbe-citations 6s5t" style="background-color:#fffaf0;"></div>
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[[Category: Pfleiderer, M.M]]
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[[Category: Galej, W.P]]
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==See Also==
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[[Category: Bhogaraju, S]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Legionella pneumophila]]
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[[Category: Adams M]]
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[[Category: Bhogaraju S]]
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[[Category: Galej WP]]
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[[Category: Pfleiderer MM]]

Current revision

Legionella pneumophila SidJ-Human calmodulin complex

6s5t, resolution 4.15Å

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