6POM

Cryo-EM structure of the full-length Bacillus subtilis glyQS T-box riboswitch in complex with tRNA-Gly

6POM の概要

• エントリーDOI: 10.2210/pdb6pom/pdb
• 関連するPDBエントリー: 6PMO
• EMDBエントリー: 20416
• 分子名称: T-box GlyQS leader (155-MER), tRNAGly (75-MER) (2 entities in total)
• 機能のキーワード: rna complex, riboswitch, transcription attenuation, stacking., rna
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78886.89

構造登録者

Li, S.,Su, Z.,Zhang, J.,Chiu, W. (登録日: 2019-07-04, 公開日: 2019-11-20, 最終更新日: 2024-03-20)

主引用文献

Li, S.,Su, Z.,Lehmann, J.,Stamatopoulou, V.,Giarimoglou, N.,Henderson, F.E.,Fan, L.,Pintilie, G.D.,Zhang, K.,Chen, M.,Ludtke, S.J.,Wang, Y.X.,Stathopoulos, C.,Chiu, W.,Zhang, J.
Structural basis of amino acid surveillance by higher-order tRNA-mRNA interactions.
Nat.Struct.Mol.Biol., 26:1094-1105, 2019

PubMed Abstract: Amino acid availability in Gram-positive bacteria is monitored by T-box riboswitches. T-boxes directly bind tRNAs, assess their aminoacylation state, and regulate the transcription or translation of downstream genes to maintain nutritional homeostasis. Here, we report cocrystal and cryo-EM structures of Geobacillus kaustophilus and Bacillus subtilis T-box-tRNA complexes, detailing their multivalent, exquisitely selective interactions. The T-box forms a U-shaped molecular vise that clamps the tRNA, captures its 3' end using an elaborate 'discriminator' structure, and interrogates its aminoacylation state using a steric filter fashioned from a wobble base pair. In the absence of aminoacylation, T-boxes clutch tRNAs and form a continuously stacked central spine, permitting transcriptional readthrough or translation initiation. A modeled aminoacyl disrupts tRNA-T-box stacking, severing the central spine and blocking gene expression. Our data establish a universal mechanism of amino acid sensing on tRNAs and gene regulation by T-box riboswitches and exemplify how higher-order RNA-RNA interactions achieve multivalency and specificity.

PubMed: 31740854
DOI: 10.1038/s41594-019-0326-7

実験手法

ELECTRON MICROSCOPY (4.9 Å)