期刊
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 79
卷 79, 期 -, 页码 381-412出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060408-173330
关键词
cryo-EM; FRET; protein synthesis; ribosome; X-ray
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM084288, R37GM029169, R01GM029169, R01GM055440] Funding Source: NIH RePORTER
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R01 GM084288, R01 GM55440, R37 GM029169, R37GM29169, R01 GM029169-29, R01 GM055440, R01 GM029169] Funding Source: Medline
There is mounting evidence indicating that protein synthesis is driven and regulated by mechanisms that direct stochastic, large-scale conformational fluctuations of the translational apparatus. This mechanistic paradigm implies that a free-energy landscape governs the conformational states that are accessible to and sampled by the translating ribosome. This scenario presents interdependent opportunities and challenges for structural and dynamic studies of protein synthesis. Indeed, the synergism between cryogenic electron microscopic and X-ray crystallographic structural studies, on the one hand, and single-molecule fluorescence resonance energy transfer (smFRET) dynamic studies, on the other, is emerging as a powerful means for investigating the complex free-energy landscape of the translating ribosome and uncovering the mechanisms that direct the stochastic conformational fluctuations of the translational machinery. In this review, we highlight the principal insights obtained from cryogenic electron microscopic, X-ray crystallographic, and smFRET studies of the elongation stage of protein synthesis and outline the emerging themes, questions, and challenges that lie ahead in mechanistic studies of translation.
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