6DRH
ADP-ribosyltransferase toxin/immunity pair
Summary for 6DRH
Entry DOI | 10.2210/pdb6drh/pdb |
Descriptor | ADP-ribosyl-(Dinitrogen reductase) hydrolase, PAAR repeat-containing protein, PHOSPHATE ION, ... (5 entities in total) |
Functional Keywords | toxin, immunity, type vi secretion, adp-ribosyltransferase |
Biological source | Serratia proteamaculans (strain 568) More |
Total number of polymer chains | 8 |
Total formula weight | 247668.74 |
Authors | Bosch, D.E.,Ting, S.,Allaire, M.,Mougous, J.D. (deposition date: 2018-06-11, release date: 2018-10-31, Last modification date: 2023-10-11) |
Primary citation | Ting, S.Y.,Bosch, D.E.,Mangiameli, S.M.,Radey, M.C.,Huang, S.,Park, Y.J.,Kelly, K.A.,Filip, S.K.,Goo, Y.A.,Eng, J.K.,Allaire, M.,Veesler, D.,Wiggins, P.A.,Peterson, S.B.,Mougous, J.D. Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins. Cell, 175:1380-, 2018 Cited by PubMed Abstract: ADP-ribosylation of proteins can profoundly impact their function and serves as an effective mechanism by which bacterial toxins impair eukaryotic cell processes. Here, we report the discovery that bacteria also employ ADP-ribosylating toxins against each other during interspecies competition. We demonstrate that one such toxin from Serratia proteamaculans interrupts the division of competing cells by modifying the essential bacterial tubulin-like protein, FtsZ, adjacent to its protomer interface, blocking its capacity to polymerize. The structure of the toxin in complex with its immunity determinant revealed two distinct modes of inhibition: active site occlusion and enzymatic removal of ADP-ribose modifications. We show that each is sufficient to support toxin immunity; however, the latter additionally provides unprecedented broad protection against non-cognate ADP-ribosylating effectors. Our findings reveal how an interbacterial arms race has produced a unique solution for safeguarding the integrity of bacterial cell division machinery against inactivating post-translational modifications. PubMed: 30343895DOI: 10.1016/j.cell.2018.09.037 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.299 Å) |
Structure validation
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