Summary for 5LI0
| Entry DOI | 10.2210/pdb5li0/pdb |
| EMDB information | 4050 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (54 entities in total) |
| Functional Keywords | pathogenic ribosome, bl31 b-type, ribosome |
| Biological source | Staphylococcus aureus (strain NCTC 8325) More |
| Total number of polymer chains | 50 |
| Total formula weight | 2097739.57 |
| Authors | Khusainov, I.,Vicens, Q.,Bochler, A.,Grosse, F.,Myasnikov, A.,Menetret, J.F.,Chicher, J.,Marzi, S.,Romby, P.,Yusupova, G.,Yusupov, M.,Hashem, Y. (deposition date: 2016-07-13, release date: 2016-12-28, Last modification date: 2024-05-15) |
| Primary citation | Khusainov, I.,Vicens, Q.,Bochler, A.,Grosse, F.,Myasnikov, A.,Menetret, J.F.,Chicher, J.,Marzi, S.,Romby, P.,Yusupova, G.,Yusupov, M.,Hashem, Y. Structure of the 70S ribosome from human pathogen Staphylococcus aureus. Nucleic Acids Res., 44:10491-10504, 2016 Cited by PubMed Abstract: Comparative structural studies of ribosomes from various organisms keep offering exciting insights on how species-specific or environment-related structural features of ribosomes may impact translation specificity and its regulation. Although the importance of such features may be less obvious within more closely related organisms, their existence could account for vital yet species-specific mechanisms of translation regulation that would involve stalling, cell survival and antibiotic resistance. Here, we present the first full 70S ribosome structure from Staphylococcus aureus, a Gram-positive pathogenic bacterium, solved by cryo-electron microscopy. Comparative analysis with other known bacterial ribosomes pinpoints several unique features specific to S. aureus around a conserved core, at both the protein and the RNA levels. Our work provides the structural basis for the many studies aiming at understanding translation regulation in S. aureus and for designing drugs against this often multi-resistant pathogen. PubMed: 27906650DOI: 10.1093/nar/gkw933 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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