The Complete Structure of the Mycobacterium smegmatis 70S Ribosome

Publication date: 5 July 2017
Source:Cell Reports, Volume 20, Issue 1
Author(s): Jendrik Hentschel, Chloe Burnside, Ingrid Mignot, Marc Leibundgut, Daniel Boehringer, Nenad Ban
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.

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Teaser

The M. tuberculosis ribosome is an important target for antibiotics in anti-tubercular therapy. Hentschel et al. determine the high-resolution structure of the related Mycobacterium smegmatis ribosome and provide a structural framework for antibiotic development and for the understanding of species-specific peculiarities of translation in Actinobacteria.


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