6ep5: Difference between revisions

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 ==Enterococcus faecalis FIC protein in complex with ADP.==
-<StructureSection load='6ep5' size='340' side='right' caption='[[6ep5]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
+<StructureSection load='6ep5' size='340' side='right'caption='[[6ep5]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ep5]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EP5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ep5]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EP5 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D350_01176 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ep5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ep5 OCA], [http://pdbe.org/6ep5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ep5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ep5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ep5 ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+FIC proteins regulate molecular processes from bacteria to humans by catalyzing post-translational modifications (PTM), the most frequent being the addition of AMP or AMPylation. In many AMPylating FIC proteins, a structurally conserved glutamate represses AMPylation and, in mammalian FICD, also supports deAMPylation of BiP/GRP78, a key chaperone of the unfolded protein response. Currently, a direct signal regulating these FIC proteins has not been identified. Here, we use X-ray crystallography and in vitro PTM assays to address this question. We discover that Enterococcus faecalis FIC (EfFIC) catalyzes both AMPylation and deAMPylation and that the glutamate implements a multi-position metal switch whereby Mg(2+) and Ca(2+) control AMPylation and deAMPylation differentially without a conformational change. Remarkably, Ca(2+) concentration also tunes deAMPylation of BiP by human FICD. Our results suggest that the conserved glutamate is a signature of AMPylation/deAMPylation FIC bifunctionality and identify metal ions as diffusible signals that regulate such FIC proteins directly.
+A Ca(2+)-regulated deAMPylation switch in human and bacterial FIC proteins.,Veyron S, Oliva G, Rolando M, Buchrieser C, Peyroche G, Cherfils J Nat Commun. 2019 Mar 8;10(1):1142. doi: 10.1038/s41467-019-09023-1. PMID:30850593<ref>PMID:30850593</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6ep5" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]]
+[[Category: Large Structures]]
 [[Category: Cherfils, J]]
 [[Category: Veyron, S]]
 [[Category: Toxin]]