6er8
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Enterococcus faecalis FIC protein in complex with phosphate.== | ==Enterococcus faecalis FIC protein in complex with phosphate.== | ||
| - | <StructureSection load='6er8' size='340' side='right' caption='[[6er8]], [[Resolution|resolution]] 2.29Å' scene=''> | + | <StructureSection load='6er8' size='340' side='right'caption='[[6er8]], [[Resolution|resolution]] 2.29Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6er8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ER8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ER8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6er8]] is a 2 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=6ER8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ER8 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A6B47_14470 ([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=6er8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6er8 OCA], [http://pdbe.org/6er8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6er8 RCSB], [http://www.ebi.ac.uk/pdbsum/6er8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6er8 ProSAT]</span></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=6er8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6er8 OCA], [http://pdbe.org/6er8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6er8 RCSB], [http://www.ebi.ac.uk/pdbsum/6er8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6er8 ProSAT]</span></td></tr> | ||
</table> | </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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6er8" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Fic protein 3D structures|Fic protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Cherfils, J]] | [[Category: Cherfils, J]] | ||
[[Category: Veyron, S]] | [[Category: Veyron, S]] | ||
Revision as of 15:53, 28 August 2019
Enterococcus faecalis FIC protein in complex with phosphate.
| |||||||||||
