The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services

Simon A. Fromm, Kate M. O’Connor, Michael Purdy, Pramod R. Bhatt, Gary Loughran, John F. Atkins (), Ahmad Jomaa () and Simone Mattei ()
Additional contact information
Simon A. Fromm: European Molecular Biology Laboratory
Kate M. O’Connor: University College Cork
Michael Purdy: University of Virginia
Pramod R. Bhatt: University College Cork
Gary Loughran: University College Cork
John F. Atkins: University College Cork
Ahmad Jomaa: University of Virginia
Simone Mattei: European Molecular Biology Laboratory

Nature Communications, 2023, vol. 14, issue 1, 1-9

Abstract: Abstract Our understanding of protein synthesis has been conceptualised around the structure and function of the bacterial ribosome. This complex macromolecular machine is the target of important antimicrobial drugs, an integral line of defence against infectious diseases. Here, we describe how open access to cryo-electron microscopy facilities combined with bespoke user support 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 enable 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.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-023-36742-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36742-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-36742-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().