7XUX
Crystal structure of a FIC domain containnig protein
Summary for 7XUX
| Entry DOI | 10.2210/pdb7xux/pdb |
| Descriptor | Fido domain-containing protein (1 entity in total) |
| Functional Keywords | fic domain protein, toxin |
| Biological source | Yersinia pseudotuberculosis serotype I (strain IP32953) |
| Total number of polymer chains | 2 |
| Total formula weight | 85449.44 |
| Authors | Zhen, X.,Ouyang, S. (deposition date: 2022-05-20, release date: 2022-12-21, Last modification date: 2024-05-29) |
| Primary citation | Wang, D.,Zhu, L.,Zhen, X.,Yang, D.,Li, C.,Chen, Y.,Wang, H.,Qu, Y.,Liu, X.,Yin, Y.,Gu, H.,Xu, L.,Wan, C.,Wang, Y.,Ouyang, S.,Shen, X. A secreted effector with a dual role as a toxin and as a transcriptional factor. Nat Commun, 13:7779-7779, 2022 Cited by PubMed Abstract: Bacteria have evolved multiple secretion systems for delivering effector proteins into the cytosol of neighboring cells, but the roles of many of these effectors remain unknown. Here, we show that Yersinia pseudotuberculosis secretes an effector, CccR, that can act both as a toxin and as a transcriptional factor. The effector is secreted by a type VI secretion system (T6SS) and can enter nearby cells of the same species and other species (such as Escherichia coli) via cell-cell contact and in a contact-independent manner. CccR contains an N-terminal FIC domain and a C-terminal DNA-binding domain. In Y. pseudotuberculosis cells, CccR inhibits its own expression by binding through its DNA-binding domain to the cccR promoter, and affects the expression of other genes through unclear mechanisms. In E. coli cells, the FIC domain of CccR AMPylates the cell division protein FtsZ, inducing cell filamentation and growth arrest. Thus, our results indicate that CccR has a dual role, modulating gene expression in neighboring cells of the same species, and inhibiting the growth of competitors. PubMed: 36522324DOI: 10.1038/s41467-022-35522-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.78 Å) |
Structure validation
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