5nwf: Difference between revisions
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<StructureSection load='5nwf' size='340' side='right'caption='[[5nwf]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5nwf' size='340' side='right'caption='[[5nwf]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nwf]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5nwf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NWF FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwf OCA], [https://pdbe.org/5nwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nwf RCSB], [https://www.ebi.ac.uk/pdbsum/5nwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/U6S0Y1_ENTFL U6S0Y1_ENTFL] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5nwf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5nwf" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Fic protein 3D structures|Fic protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enterococcus | [[Category: Enterococcus faecalis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cherfils | [[Category: Cherfils J]] | ||
[[Category: Veyron | [[Category: Veyron S]] | ||
Latest revision as of 15:12, 22 November 2023
Enterococcus faecalis FIC protein (H111A).Enterococcus faecalis FIC protein (H111A).
Structural highlights
FunctionPublication Abstract from PubMedFIC 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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