6ER8
Enterococcus faecalis FIC protein in complex with phosphate.
6ER8 の概要
| エントリーDOI | 10.2210/pdb6er8/pdb |
| 分子名称 | Fic family protein, ACETATE ION, PHOSPHATE ION, ... (4 entities in total) |
| 機能のキーワード | fic, ampylation, toxin |
| 由来する生物種 | Enterococcus faecalis |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 49521.22 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.292 Å) |
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