7rt7

Crystal structure of the RhsP2 C-terminal toxin domain in complex with its immunity protein, RhsI2

spinqualitylabelsall models 7rt7, resolution 2.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7rt7 is a 12 chain structure with sequence from Pseudomonas aeruginosa UCBPP-PA14. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.49Å Ligands: TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2Z8A2_PSEAB Publication Abstract from PubMed ADP-ribosyltransferases (ARTs) were among the first identified bacterial virulence factors. Canonical ART toxins are delivered into host cells where they modify essential proteins, thereby inactivating cellular processes and promoting pathogenesis. Our understanding of ARTs has since expanded beyond protein-targeting toxins to include antibiotic inactivation and DNA damage repair. Here, we report the discovery of RhsP2 as an ART toxin delivered between competing bacteria by a type VI secretion system of Pseudomonas aeruginosa. A structure of RhsP2 reveals that it resembles protein-targeting ARTs such as diphtheria toxin. Remarkably, however, RhsP2 ADP-ribosylates 2'-hydroxyl groups of double-stranded RNA, and thus, its activity is highly promiscuous with identified cellular targets including the tRNA pool and the RNA-processing ribozyme, ribonuclease P. Consequently, cell death arises from the inhibition of translation and disruption of tRNA processing. Overall, our data demonstrate a previously undescribed mechanism of bacterial antagonism and uncover an unprecedented activity catalyzed by ART enzymes. An ADP-ribosyltransferase toxin kills bacterial cells by modifying structured non-coding RNAs.,Bullen NP, Sychantha D, Thang SS, Culviner PH, Rudzite M, Ahmad S, Shah VS, Filloux A, Prehna G, Whitney JC Mol Cell. 2022 Sep 15;82(18):3484-3498.e11. doi: 10.1016/j.molcel.2022.08.015. , Epub 2022 Sep 6. PMID:36070765 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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