9XTD

E.coli delta lepA 30S ribosomal subunit class B, body domain

9XTD の概要

• エントリーDOI: 10.2210/pdb9xtd/pdb
• EMDBエントリー: 67202
• 分子名称: RNA (1128-MER), Small ribosomal subunit protein uS17, Small ribosomal subunit protein bS18, ... (15 entities in total)
• 機能のキーワード: 30s subunit maturation, lepa, cryo-em, ribosome assembly, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 662796.65

構造登録者

Kravchenko, O.V.,Maksimova, E.M.,Baymukhametov, T.N.,Stolboushkina, E.A. (登録日: 2025-11-22, 公開日: 2026-04-08)

主引用文献

Kravchenko, O.,Maksimova, E.,Baymukhametov, T.,Eliseeva, I.,Stolboushkina, E.
The Conserved GTPase LepA May Contribute to the Final Proper Stabilization of the 3' Domain of the 30S Subunit During Ribosome Assembly.
Int J Mol Sci, 27:-, 2026

PubMed Abstract: The function of the highly conserved GTPase LepA, a homolog of elongation factor EF-G, remains unknown in translation. However, there is biochemical data that it implicates in the 30S ribosomal subunit biogenesis. Here, using cryo-electron microscopy, we characterized 30S subunits isolated from an strain with a deleted gene. The cryo-EM maps for ∆ 30S particles were divided into classes corresponding to consecutive assembly intermediates: from particles characterized by unformed helices h44/h45 of the central decoding center (CDR) and highly flexible head, through intermediates with a distorted CDR and a partial stabilization of the head, to near-mature 30S subunits with correctly docked h44 in the CDR, accessible 3' end of 16S rRNA for translation but significant flexibility in head domain. Cryo-EM analysis of Δ 30S intermediates revealed that they predominantly proceed to nearly mature functional state and exhibit suboptimal flexibility in the head domain. This finding suggests that LepA likely contributes to the final proper stabilization of the 3' domain of the 30S subunit during ribosome assembly.

PubMed: 41516366
DOI: 10.3390/ijms27010489

実験手法

ELECTRON MICROSCOPY (2.26 Å)