6EP0
Enterococcus faecalis FIC protein in complex with AMP and calcium ion.
Summary for 6EP0
| Entry DOI | 10.2210/pdb6ep0/pdb |
| Related | 5NUW |
| Descriptor | Fic family protein, ADENOSINE MONOPHOSPHATE, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | toxin |
| Biological source | Enterococcus faecalis |
| Total number of polymer chains | 2 |
| Total formula weight | 50278.05 |
| Authors | Veyron, S.,Cherfils, J. (deposition date: 2017-10-10, release date: 2019-02-06, Last modification date: 2024-01-17) |
| Primary citation | Veyron, S.,Oliva, G.,Rolando, M.,Buchrieser, C.,Peyroche, G.,Cherfils, J. A Ca2+-regulated deAMPylation switch in human and bacterial FIC proteins. Nat Commun, 10:1142-1142, 2019 Cited by PubMed Abstract: 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 and Ca control AMPylation and deAMPylation differentially without a conformational change. Remarkably, Ca 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. PubMed: 30850593DOI: 10.1038/s41467-019-09023-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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