5O61
The complete structure of the Mycobacterium smegmatis 70S ribosome
This is a non-PDB format compatible entry.
Summary for 5O61
| Entry DOI | 10.2210/pdb5o61/pdb | 
| Related | 5O5J 5O60 | 
| EMDB information | 3748 3750 3751 | 
| Descriptor | 50S ribosomal protein bL37, 50S ribosomal protein L10, 50S ribosomal protein L11, ... (60 entities in total) | 
| Functional Keywords | ribosome, translation | 
| Biological source | Mycobacterium smegmatis str. MC2 155 More  | 
| Total number of polymer chains | 57 | 
| Total formula weight | 2322203.63 | 
| Authors | Hentschel, J.,Burnside, C.,Mignot, I.,Leibundgut, M.,Boehringer, D.,Ban, N. (deposition date: 2017-06-03, release date: 2017-07-12, Last modification date: 2024-05-15)  | 
| Primary citation | Hentschel, J.,Burnside, C.,Mignot, I.,Leibundgut, M.,Boehringer, D.,Ban, N. The Complete Structure of the Mycobacterium smegmatis 70S Ribosome. Cell Rep, 20:149-160, 2017 Cited by  PubMed Abstract: The ribosome carries out the synthesis of proteins in every living cell. It consequently represents a frontline target in anti-microbial therapy. Tuberculosis ranks among the leading causes of death worldwide, due in large part to the combination of difficult-to-treat latency and antibiotic resistance. Here, we present the 3.3-Å cryo-EM structure of the 70S ribosome of Mycobacterium smegmatis, a close relative to the human pathogen Mycobacterium tuberculosis. The structure reveals two additional ribosomal proteins and localizes them to the vicinity of drug-target sites in both the catalytic center and the decoding site of the ribosome. Furthermore, we visualized actinobacterium-specific rRNA and protein expansions that extensively remodel the ribosomal surface with implications for polysome organization. Our results provide a foundation for understanding the idiosyncrasies of mycobacterial translation and reveal atomic details of the structure that will facilitate the design of anti-tubercular therapeutics. PubMed: 28683309DOI: 10.1016/j.celrep.2017.06.029 PDB entries with the same primary citation  | 
| Experimental method | ELECTRON MICROSCOPY (3.31 Å)  | 
Structure validation
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