5WNQ

Crystal Structure of 30S ribosomal subunit from Thermus thermophilus

5WNQ の概要

• エントリーDOI: 10.2210/pdb5wnq/pdb
• 分子名称: 16S Ribosomal RNA rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (24 entities in total)
• 機能のキーワード: smfret, ribosome, mrna methylation, translation, decoding
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 772093.98

構造登録者

DeMirci, H. (登録日: 2017-08-01, 公開日: 2018-02-21, 最終更新日: 2020-10-21)

主引用文献

Choi, J.,Indrisiunaite, G.,DeMirci, H.,Ieong, K.W.,Wang, J.,Petrov, A.,Prabhakar, A.,Rechavi, G.,Dominissini, D.,He, C.,Ehrenberg, M.,Puglisi, J.D.
2'-O-methylation in mRNA disrupts tRNA decoding during translation elongation.
Nat. Struct. Mol. Biol., 25:208-216, 2018

PubMed Abstract: Chemical modifications of mRNA may regulate many aspects of mRNA processing and protein synthesis. Recently, 2'-O-methylation of nucleotides was identified as a frequent modification in translated regions of human mRNA, showing enrichment in codons for certain amino acids. Here, using single-molecule, bulk kinetics and structural methods, we show that 2'-O-methylation within coding regions of mRNA disrupts key steps in codon reading during cognate tRNA selection. Our results suggest that 2'-O-methylation sterically perturbs interactions of ribosomal-monitoring bases (G530, A1492 and A1493) with cognate codon-anticodon helices, thereby inhibiting downstream GTP hydrolysis by elongation factor Tu (EF-Tu) and A-site tRNA accommodation, leading to excessive rejection of cognate aminoacylated tRNAs in initial selection and proofreading. Our current and prior findings highlight how chemical modifications of mRNA tune the dynamics of protein synthesis at different steps of translation elongation.

PubMed: 29459784
DOI: 10.1038/s41594-018-0030-z

実験手法

X-RAY DIFFRACTION (3.5 Å)