8A3L

Structural insights into the binding of bS1 to the ribosome

This is a non-PDB format compatible entry.

Summary for 8A3L

• Entry DOI: 10.2210/pdb8a3l/pdb
• EMDB information: 15116
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (58 entities in total)
• Functional Keywords: bs1, ribosome, cryo-em, translation
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 56
• Total formula weight: 2265477.73

Authors

D'Urso, G.,Chat, S.,Gillet, R.,Giudice, E. (deposition date: 2022-06-08, release date: 2023-05-10, Last modification date: 2025-03-12)

Primary citation

D'Urso, G.,Chat, S.,Gillet, R.,Giudice, E.
Structural insights into the binding of bS1 to the ribosome.
Nucleic Acids Res., 51:3410-3419, 2023

PubMed Abstract: The multidomain ribosomal protein bS1 is the biggest and the most flexible and dynamic protein in the 30S small subunit. Despite being essential for mRNA recruitment and its primary role in the accommodation of the start codon within the decoding centre, there has not yet been a high-resolution description of its structure. Here, we present a 3D atomic model of OB1 and OB2, bS1's first two N-terminal domains, bound to an elongation-competent 70S ribosome. Our structure reveals that, as previously reported, bS1 is anchored both by a π-stacking to the 30S subunit and via a salt bridge with the Zn2+ pocket of bS1. These contacts are further stabilized by other interactions with additional residues on OB1. Our model also shows a new conformation of OB2, interacting with the Shine-Dalgarno portion of the mRNA. This study confirms that OB1 plays an anchoring role, but also highlights a novel function for OB2, which is directly involved in the modulation and support of mRNA binding and accommodation on the ribosome.

PubMed: 36840711
DOI: 10.1093/nar/gkad126

Experimental method

ELECTRON MICROSCOPY (3.42 Å)