7V2L

T.thermophilus 30S ribosome with KsgA, class K1k2

7V2L の概要

• エントリーDOI: 10.2210/pdb7v2l/pdb
• EMDBエントリー: 31655 31656 31657 31658 31659 31660
• 分子名称: 16s ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (23 entities in total)
• 機能のキーワード: 30s subunit, ksga, rrna methyltransferase, ribosome
• 由来する生物種: Bacillus subtilis (strain 168); 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 817114.25

構造登録者

Raina, R.,Singh, J.,Anand, R.,Vinothkumar, K.R. (登録日: 2021-08-09, 公開日: 2022-04-06, 最終更新日: 2024-06-12)

主引用文献

Singh, J.,Raina, R.,Vinothkumar, K.R.,Anand, R.
Decoding the Mechanism of Specific RNA Targeting by Ribosomal Methyltransferases.
Acs Chem.Biol., 17:829-839, 2022

PubMed Abstract: Methylation of specific nucleotides is integral for ribosomal biogenesis and also serves as a common mechanism to confer antibiotic resistance by pathogenic bacteria. Here, by determining the high-resolution structure of the 30S-KsgA complex by cryo-electron microscopy, a state was captured, where KsgA juxtaposes between helices h44 and h45 of the 30S ribosome, separating them, thereby enabling remodeling of the surrounded rRNA and allowing the cognate site to enter the methylation pocket. With the structure as a guide, several mutant versions of the ribosomes, where interacting bases in the catalytic helix h45 and surrounding helices h44, h24, and h27, were mutated and evaluated for their methylation efficiency revealing factors that direct the enzyme to its cognate site with high fidelity. The biochemical studies show that the three-dimensional environment of the ribosome enables the interaction of select loop regions in KsgA with the ribosome helices paramount to maintain selectivity.

PubMed: 35316014
DOI: 10.1021/acschembio.1c00732

実験手法

ELECTRON MICROSCOPY (3.3 Å)