4X66

Crystal Structure of 30S ribosomal subunit from Thermus thermophilus

4X66 の概要

• エントリーDOI: 10.2210/pdb4x66/pdb
• 分子名称: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (28 entities in total)
• 機能のキーワード: 30s ribosomal subunit m6a decoding mrna modification, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 23
• 化学式量合計: 785898.94

構造登録者

Demirci, H.,Chen, J.,Choi, J.,Soltis, M.,Puglisi, J.D. (登録日: 2014-12-06, 公開日: 2015-11-18, 最終更新日: 2025-02-19)

主引用文献

Choi, J.,Ieong, K.W.,Demirci, H.,Chen, J.,Petrov, A.,Prabhakar, A.,O'Leary, S.E.,Dominissini, D.,Rechavi, G.,Soltis, S.M.,Ehrenberg, M.,Puglisi, J.D.
N(6)-methyladenosine in mRNA disrupts tRNA selection and translation-elongation dynamics.
Nat.Struct.Mol.Biol., 23:110-115, 2016

PubMed Abstract: N(6)-methylation of adenosine (forming m(6)A) is the most abundant post-transcriptional modification within the coding region of mRNA, but its role during translation remains unknown. Here, we used bulk kinetic and single-molecule methods to probe the effect of m(6)A in mRNA decoding. Although m(6)A base-pairs with uridine during decoding, as shown by X-ray crystallographic analyses of Thermus thermophilus ribosomal complexes, our measurements in an Escherichia coli translation system revealed that m(6)A modification of mRNA acts as a barrier to tRNA accommodation and translation elongation. The interaction between an m(6)A-modified codon and cognate tRNA echoes the interaction between a near-cognate codon and tRNA, because delay in tRNA accommodation depends on the position and context of m(6)A within codons and on the accuracy level of translation. Overall, our results demonstrate that chemical modification of mRNA can change translational dynamics.

PubMed: 26751643
DOI: 10.1038/nsmb.3148

実験手法

X-RAY DIFFRACTION (3.446 Å)