8EYQ

30S_delta_ksgA_h44_inactive_conformation

8EYQ の概要

• エントリーDOI: 10.2210/pdb8eyq/pdb
• EMDBエントリー: 28692
• 分子名称: 30S ribosomal protein S4, 30S ribosomal protein S18, 30S ribosomal protein S20, ... (18 entities in total)
• 機能のキーワード: ribosome, ksga
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 733525.80

構造登録者

Ortega, J.,Sun, J. (登録日: 2022-10-28, 公開日: 2023-09-06, 最終更新日: 2023-11-01)

主引用文献

Sun, J.,Kinman, L.F.,Jahagirdar, D.,Ortega, J.,Davis, J.H.
KsgA facilitates ribosomal small subunit maturation by proofreading a key structural lesion.
Nat.Struct.Mol.Biol., 30:1468-1480, 2023

PubMed Abstract: Ribosome assembly is orchestrated by many assembly factors, including ribosomal RNA methyltransferases, whose precise role is poorly understood. Here, we leverage the power of cryo-EM and machine learning to discover that the E. coli methyltransferase KsgA performs a 'proofreading' function in the assembly of the small ribosomal subunit by recognizing and partially disassembling particles that have matured but are not competent for translation. We propose that this activity allows inactive particles an opportunity to reassemble into an active state, thereby increasing overall assembly fidelity. Detailed structural quantifications in our datasets additionally enabled the expansion of the Nomura assembly map to highlight rRNA helix and r-protein interdependencies, detailing how the binding and docking of these elements are tightly coupled. These results have wide-ranging implications for our understanding of the quality-control mechanisms governing ribosome biogenesis and showcase the power of heterogeneity analysis in cryo-EM to unveil functionally relevant information in biological systems.

PubMed: 37653244
DOI: 10.1038/s41594-023-01078-5

実験手法

ELECTRON MICROSCOPY (3.3 Å)