7NBU
Structure of the HigB1 toxin mutant K95A from Mycobacterium tuberculosis (Rv1955) and its target, the cspA mRNA, on the E. coli Ribosome.
This is a non-PDB format compatible entry.
Summary for 7NBU
| Entry DOI | 10.2210/pdb7nbu/pdb |
| Related | 7awk |
| EMDB information | 12261 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total) |
| Functional Keywords | toxin |
| Biological source | Mycobacterium tuberculosis H37Rv More |
| Total number of polymer chains | 56 |
| Total formula weight | 2155043.20 |
| Authors | Giudice, E.,Mansour, M.,Chat, S.,D'Urso, G.,Gillet, R.,Genevaux, P. (deposition date: 2021-01-27, release date: 2022-03-02, Last modification date: 2024-04-24) |
| Primary citation | Mansour, M.,Giudice, E.,Xu, X.,Akarsu, H.,Bordes, P.,Guillet, V.,Bigot, D.J.,Slama, N.,D'urso, G.,Chat, S.,Redder, P.,Falquet, L.,Mourey, L.,Gillet, R.,Genevaux, P. Substrate recognition and cryo-EM structure of the ribosome-bound TAC toxin of Mycobacterium tuberculosis. Nat Commun, 13:2641-2641, 2022 Cited by PubMed Abstract: Toxins of toxin-antitoxin systems use diverse mechanisms to control bacterial growth. Here, we focus on the deleterious toxin of the atypical tripartite toxin-antitoxin-chaperone (TAC) system of Mycobacterium tuberculosis, whose inhibition requires the concerted action of the antitoxin and its dedicated SecB-like chaperone. We show that the TAC toxin is a bona fide ribonuclease and identify exact cleavage sites in mRNA targets on a transcriptome-wide scale in vivo. mRNA cleavage by the toxin occurs after the second nucleotide of the ribosomal A-site codon during translation, with a strong preference for CCA codons in vivo. Finally, we report the cryo-EM structure of the ribosome-bound TAC toxin in the presence of native M. tuberculosis cspA mRNA, revealing the specific mechanism by which the TAC toxin interacts with the ribosome and the tRNA in the P-site to cleave its mRNA target. PubMed: 35552387DOI: 10.1038/s41467-022-30373-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.11 Å) |
Structure validation
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