5O60
Structure of the 50S large ribosomal subunit from Mycobacterium smegmatis
Summary for 5O60
Entry DOI | 10.2210/pdb5o60/pdb |
Related | 5O5J 5O61 |
EMDB information | 3748 3750 3751 |
Descriptor | 50S ribosomal protein bL37, 50S ribosomal protein L10, 50S ribosomal protein L11, ... (38 entities in total) |
Functional Keywords | ribosome, translation |
Biological source | Mycobacterium smegmatis str. MC2 155 More |
Total number of polymer chains | 35 |
Total formula weight | 1496821.68 |
Authors | Hentschel, J.,Burnside, C.,Mignot, I.,Leibundgut, M.,Boehringer, D.,Ban, N. (deposition date: 2017-06-02, 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 (3.18 Å) |
Structure validation
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