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7D8O

Crystal structure of E. coli ToxIN type III toxin-antitoxin complex

Summary for 7D8O
Entry DOI10.2210/pdb7d8o/pdb
DescriptorType III toxin-antitoxin system ToxN/AbiQ family toxin, Antitoxin RNA (3 entities in total)
Functional Keywordstoxin-antitoxin complex, toxin, endoribonuclease, rna pseudoknot, rna-protein complex, toxin-rna complex, toxin/rna
Biological sourceEscherichia coli
More
Total number of polymer chains12
Total formula weight201695.89
Authors
Manikandan, P.,Rothweiler, U.,Singh, M. (deposition date: 2020-10-08, release date: 2022-01-05, Last modification date: 2023-11-29)
Primary citationManikandan, P.,Sandhya, S.,Nadig, K.,Paul, S.,Srinivasan, N.,Rothweiler, U.,Singh, M.
Identification, functional characterization, assembly and structure of ToxIN type III toxin-antitoxin complex from E. coli.
Nucleic Acids Res., 50:1687-1700, 2022
Cited by
PubMed Abstract: Toxin-antitoxin (TA) systems are proposed to play crucial roles in bacterial growth under stress conditions such as phage infection. The type III TA systems consist of a protein toxin whose activity is inhibited by a noncoding RNA antitoxin. The toxin is an endoribonuclease, while the antitoxin consists of multiple repeats of RNA. The toxin assembles with the individual antitoxin repeats into a cyclic complex in which the antitoxin forms a pseudoknot structure. While structure and functions of some type III TA systems are characterized, the complex assembly process is not well understood. Using bioinformatics analysis, we have identified type III TA systems belonging to the ToxIN family across different Escherichia coli strains and found them to be clustered into at least five distinct clusters. Furthermore, we report a 2.097 Å resolution crystal structure of the first E. coli ToxIN complex that revealed the overall assembly of the protein-RNA complex. Isothermal titration calorimetry experiments showed that toxin forms a high-affinity complex with antitoxin RNA resulting from two independent (5' and 3' sides of RNA) RNA binding sites on the protein. These results further our understanding of the assembly of type III TA complexes in bacteria.
PubMed: 35018473
DOI: 10.1093/nar/gkab1264
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.097 Å)
Structure validation

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