8rr6

MenT3 (aka TglT) toxin (Rv1045) from Mycobacterium tuberculosis H37Rv, non-phosphorylated

spinqualitylabelsall models 8rr6, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8rr6 is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.78Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P96356_MYCTU Publication Abstract from PubMed Nucleotidyltransferases (NTases) control diverse physiological processes, including RNA modification, DNA replication and repair, and antibiotic resistance. The Mycobacterium tuberculosis NTase toxin family, MenT, modifies tRNAs to block translation. MenT toxin activity can be stringently regulated by diverse MenA antitoxins. There has been no unifying mechanism linking antitoxicity across MenT homologues. Here we demonstrate through structural, biochemical, biophysical and computational studies that despite lacking kinase motifs, antitoxin MenA(1) induces auto-phosphorylation of MenT(1) by repositioning the MenT(1) phosphoacceptor T39 active site residue towards bound nucleotide. Finally, we expand this predictive model to explain how unrelated antitoxin MenA(3) is similarly able to induce auto-phosphorylation of cognate toxin MenT(3). Our study reveals a conserved mechanism for the control of tuberculosis toxins, and demonstrates how active site auto-phosphorylation can regulate the activity of widespread NTases. Inducible auto-phosphorylation regulates a widespread family of nucleotidyltransferase toxins.,Arrowsmith TJ, Xu X, Xu S, Usher B, Stokes P, Guest M, Bronowska AK, Genevaux P, Blower TR Nat Commun. 2024 Sep 4;15(1):7719. doi: 10.1038/s41467-024-51934-1. PMID:39231966 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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