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6DRH

ADP-ribosyltransferase toxin/immunity pair

Summary for 6DRH
Entry DOI10.2210/pdb6drh/pdb
DescriptorADP-ribosyl-(Dinitrogen reductase) hydrolase, PAAR repeat-containing protein, PHOSPHATE ION, ... (5 entities in total)
Functional Keywordstoxin, immunity, type vi secretion, adp-ribosyltransferase
Biological sourceSerratia proteamaculans (strain 568)
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Total number of polymer chains8
Total formula weight247668.74
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 citationTing, 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: 30343895
DOI: 10.1016/j.cell.2018.09.037
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.299 Å)
Structure validation

227111

数据于2024-11-06公开中

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