9BSL

45SRbgA particle in complex with RbgA and YphC. Class A

9BSL の概要

• エントリーDOI: 10.2210/pdb9bsl/pdb
• EMDBエントリー: 44869
• 分子名称: 23S rRNA, Large ribosomal subunit protein bL19, Large ribosomal subunit protein bL20, ... (23 entities in total)
• 機能のキーワード: ribosome, ribosome assembly, yphc
• 由来する生物種: Bacillus subtilis subsp. subtilis str. 168; 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 1309822.68

構造登録者

Arpin, D.,Ortega, J. (登録日: 2024-05-13, 公開日: 2024-12-25, 最終更新日: 2025-05-28)

主引用文献

Arpin, D.,Palacios, A.,Basu, K.,Ortega, J.
The binding of RbgA to a critical 50S assembly intermediate facilitates YphC function in bacterial ribosomal assembly.
Nucleic Acids Res., 53:-, 2025

PubMed Abstract: The intricate process of 50S ribosomal subunit assembly in Bacillus subtilis involves multiple parallel pathways converging into a crucial intermediate known as the 45S particle. RbgA and YphC, play pivotal roles in completing the maturation of the functional sites in the 45S particle. In this work, we found that RbgA and YphC can independently bind the 45S particle with high affinity, but when RbgA binds first to the particle, it significantly increases the binding affinity of YphC. Using cryo-electron microscopy, we determined that the changes exerted by RbgA and YphC when binding independently closely resemble those observed when the two factors bind to the 45S particle simultaneously. However, the structural analysis revealed that RbgA binding causes a conformational change that uncovers the binding site for YphC, thus increasing its binding affinity. We concluded that the functional interplay between RbgA and YphC primarily revolves around one factor promoting the binding of the other, rather than the binding of the two factors inducing entirely new conformational changes compared with those induced by the factors individually. These results highlight the synergic mechanism between two essential assembly factors, underscoring the intricate mechanism bacteria use to maximize the efficiency of the ribosome assembly process.

PubMed: 39658043
DOI: 10.1093/nar/gkae1197

実験手法

ELECTRON MICROSCOPY (3.1 Å)