7mis: Difference between revisions

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-====
+==Cryo-EM structure of SidJ-SdeC-CaM reaction intermediate complex==
-<StructureSection load='7mis' size='340' side='right'caption='[[7mis]]' scene=''>
+<StructureSection load='7mis' size='340' side='right'caption='[[7mis]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7mis]] is a 3 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=7MIS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MIS FirstGlance]. <br>
-</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=7mis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mis OCA], [https://pdbe.org/7mis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mis RCSB], [https://www.ebi.ac.uk/pdbsum/7mis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mis ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7mis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mis OCA], [https://pdbe.org/7mis PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mis RCSB], [https://www.ebi.ac.uk/pdbsum/7mis PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mis ProSAT]</span></td></tr>
 </table>
+== Function ==
+[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:31330531, PubMed:31330532). In turn, inhibits SdeA ubiquitinating activity. Glutamylates also related SdeB, SdeC and SidE (PubMed:31123136, PubMed:31330531). Glutamylase activity only occurs in the host since it requires host calmodulin (PubMed:28497808, PubMed:31123136, PubMed:31330531, PubMed:31330532). 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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The kinase domain transfers phosphate from ATP to substrates. However, the Legionella effector SidJ adopts a kinase fold, yet catalyzes calmodulin (CaM)-dependent glutamylation to inactivate the SidE ubiquitin ligases. The structural and mechanistic basis in which the kinase domain catalyzes protein glutamylation is unknown. Here we present cryo-EM reconstructions of SidJ:CaM:SidE reaction intermediate complexes. We show that the kinase-like active site of SidJ adenylates an active-site Glu in SidE, resulting in the formation of a stable reaction intermediate complex. An insertion in the catalytic loop of the kinase domain positions the donor Glu near the acyl-adenylate for peptide bond formation. Our structural analysis led us to discover that the SidJ paralog SdjA is a glutamylase that differentially regulates the SidE ligases during Legionella infection. Our results uncover the structural and mechanistic basis in which the kinase fold catalyzes non-ribosomal amino acid ligations and reveal an unappreciated level of SidE-family regulation.
+Structural and mechanistic basis for protein glutamylation by the kinase fold.,Osinski A, Black MH, Pawlowski K, Chen Z, Li Y, Tagliabracci VS Mol Cell. 2021 Nov 4;81(21):4527-4539.e8. doi: 10.1016/j.molcel.2021.08.007. Epub , 2021 Aug 17. PMID:34407442<ref>PMID:34407442</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7mis" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Z-disk]]
+[[Category: Legionella pneumophila]]
+[[Category: Black MH]]
+[[Category: Chen Z]]
+[[Category: Li Y]]
+[[Category: Osinski A]]
+[[Category: Pawlowski K]]
+[[Category: Tagliabracci VS]]