9ils

The GmvT toxin in complex with the C-terminal fragment of its antitoxin

spinqualitylabelsall models 9ils, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ils is a 2 chain structure with sequence from Shigella sonnei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.75Å Ligands: PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Toxin-antitoxin (TA) systems are common bicistronic gene elements in bacteria and are critical for stress responses. The toxin members of the GNAT/RHH TA family can acetylate certain aminoacylated tRNA molecules and inhibit global protein translation. One member named GmvT is important for virulence plasmid maintenance in Shigella flexneri, but the underlying mechanism remains poorly understood. Here, we report the cocrystal structures of GmvT in two forms. The binding of the antitoxin mainly relies on the backbone of the toxin while the cofactor is free of contacts with the antitoxin, supported by follow-up in vitro and in vivo studies. Our study provides insight into the protein-protein/protein-ligand interactions of the GmvAT pair and the structural basis for molecular recognition. Structural insights into the Shigella flexneri GmvAT toxin-antitoxin system.,Chen R, Zhao H, Zhou J, Liu A, Guo Y, Wu K, Xiang Y, Lei J, Jiang S, Xie W FEBS Lett. 2025 Feb 20. doi: 10.1002/1873-3468.70015. PMID:39973444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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