| Autor: |
Simon A. Fromm, Kate M. O’Connor, Michael Purdy, Pramod R. Bhatt, Gary Loughran, John F. Atkins, Ahmad Jomaa, Simone Mattei |
| Rok vydání: |
2022 |
| DOI: |
10.1101/2022.08.30.505838 |
| Popis: |
Our understanding of protein synthesis has been conceptualised around the structure and function of the bacterial ribosome1–4. This complex macromolecular machine is the target of important antimicrobial drugs5, an integral line of defence against infectious diseases. Here, we describe how open access to state-of-the-art cryogenic electron microscopy facilities combined with bespoke user support offered by the newly established EMBL Imaging Centre enabled structural determination of the translating ribosome from Escherichia coli at 1.55 Å resolution. The obtained structures allow for direct determination of the rRNA sequence to identify ribosome polymorphism sites in the E. coli strain used in this study and enables interpretation of the ribosomal active and peripheral sites at unprecedented resolution. This includes scarcely populated chimeric hybrid states of the ribosome engaged in several tRNA translocation steps resolved at ~2 Å resolution. The current map not only improves our understanding of protein synthesis but also allows for more precise structure-based drug design of antibiotics to tackle rising bacterial resistance. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
