4YY3
30S ribosomal subunit- HigB complex
Summary for 4YY3
| Entry DOI | 10.2210/pdb4yy3/pdb |
| Related | 4MCT 4MCX |
| Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (24 entities in total) |
| Functional Keywords | bacterial toxins, stringent response, translational control, rnase, ribosome |
| Biological source | Proteus vulgaris More |
| Total number of polymer chains | 22 |
| Total formula weight | 801954.02 |
| Authors | Schureck, M.A.,Maehigashi, T.,Dunham, C.M. (deposition date: 2015-03-23, release date: 2016-07-06, Last modification date: 2023-09-27) |
| Primary citation | Schureck, M.A.,Maehigashi, T.,Miles, S.J.,Marquez, J.,Dunham, C.M. mRNA bound to the 30S subunit is a HigB toxin substrate. Rna, 22:1261-1270, 2016 Cited by PubMed Abstract: Activation of bacterial toxins during stress results in cleavage of mRNAs in the context of the ribosome. These toxins are thought to function as global translational inhibitors yet recent studies suggest each may have distinct mRNA specificities that result in selective translation for bacterial survival. Here we demonstrate that mRNA in the context of a bacterial 30S subunit is sufficient for ribosome-dependent toxin HigB endonucleolytic activity, suggesting that HigB interferes with the initiation step of translation. We determined the X-ray crystal structure of HigB bound to the 30S, revealing that two solvent-exposed clusters of HigB basic residues directly interact with 30S 16S rRNA helices 18, 30, and 31. We further show that these HigB residues are essential for ribosome recognition and function. Comparison with other ribosome-dependent toxins RelE and YoeB reveals that each interacts with similar features of the 30S aminoacyl (A) site yet does so through presentation of diverse structural motifs. PubMed: 27307497DOI: 10.1261/rna.056218.116 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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