期刊
CELL REPORTS
卷 20, 期 1, 页码 149-160出版社
CELL PRESS
DOI: 10.1016/j.celrep.2017.06.029
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资金
- Boehringer Ingelheim Fonds PhD Fellowship
- Swiss National Science Foundation (SNSF) [310030B_163478]
- National Center of Excellence in Research (NCCR) RNA & Disease Program of the SNSF [51NF40_141735]
- Swiss National Science Foundation (SNF) [310030B_163478] Funding Source: Swiss National Science Foundation (SNF)
The ribosome carries out the synthesis of proteins in every living cell. It consequently represents a front-line target in anti-microbial therapy. Tuberculosis ranks among the leading causes of death worldwide, due in large part to the combination of difficult-totreat latency and antibiotic resistance. Here, we present the 3.3-angstrom 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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