8FN2

The structure of a 50S ribosomal subunit in the Lyme disease pathogen Borreliella burgdorferi

Summary for 8FN2

• Entry DOI: 10.2210/pdb8fn2/pdb
• Related: 8FMW
• EMDB information: 29298 29304
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L11, 50S ribosomal protein L13, ... (35 entities in total)
• Functional Keywords: hibernating ribosome, bacterial, pathogen, 50s, translation, ribosome
• Biological source: Borreliella burgdorferi B31; More
• Total number of polymer chains: 34
• Total formula weight: 1420668.70

Authors

Sharma, M.R.,Manjari, S.R.,Agrawal, E.K.,Keshavan, P.,Koripella, R.K.,Majumdar, S.,Marcinkiewicz, A.L.,Lin, Y.P.,Agrawal, R.K.,Banavali, N.K. (deposition date: 2022-12-26, release date: 2023-11-08, Last modification date: 2024-10-09)

Primary citation

Sharma, M.R.,Manjari, S.R.,Agrawal, E.K.,Keshavan, P.,Koripella, R.K.,Majumdar, S.,Marcinkiewicz, A.L.,Lin, Y.P.,Agrawal, R.K.,Banavali, N.K.
The structure of a hibernating ribosome in a Lyme disease pathogen.
Nat Commun, 14:6961-6961, 2023

PubMed Abstract: The spirochete bacterial pathogen Borrelia (Borreliella) burgdorferi (Bbu) affects more than 10% of the world population and causes Lyme disease in about half a million people in the US annually. Therapy for Lyme disease includes antibiotics that target the Bbu ribosome. Here we present the structure of the Bbu 70S ribosome obtained by single particle cryo-electron microscopy at 2.9 Å resolution, revealing a bound hibernation promotion factor protein and two genetically non-annotated ribosomal proteins bS22 and bL38. The ribosomal protein uL30 in Bbu has an N-terminal α-helical extension, partly resembling the mycobacterial bL37 protein, suggesting evolution of bL37 and a shorter uL30 from a longer uL30 protein. Its analogy to proteins uL30m and mL63 in mammalian mitochondrial ribosomes also suggests a plausible evolutionary pathway for expansion of protein content in mammalian mitochondrial ribosomes. Computational binding free energy predictions for antibiotics reflect subtle distinctions in antibiotic-binding sites in the Bbu ribosome. Discovery of these features in the Bbu ribosome may enable better ribosome-targeted antibiotic design for Lyme disease treatment.

PubMed: 37907464
DOI: 10.1038/s41467-023-42266-7

Experimental method

ELECTRON MICROSCOPY (3.4 Å)