4Z3S

Crystal structure of the Thermus thermophilus 70S ribosome in complex with antibiotic A201A, mRNA and three tRNAs in the A, P and E sites at 2.65A resolution

これはPDB形式変換不可エントリーです。

4Z3S の概要

• エントリーDOI: 10.2210/pdb4z3s/pdb
• 関連するPDBエントリー: 4Z3Q 4Z3R
• 分子名称: 23S Ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (62 entities in total)
• 機能のキーワード: hygromycin a, a201a, antibiotic, 70s ribosome, inhibition of translation, peptidyl transferase inhibitors, trna accommodation intermediate, single-molecule fret, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 112
• 化学式量合計: 4562038.37

構造登録者

Polikanov, Y.S.,Starosta, A.L.,Juette, M.F.,Altman, R.B.,Terry, D.S.,Lu, W.,Burnett, B.J.,Dinos, G.,Reynolds, K.,Blanchard, S.C.,Steitz, T.A.,Wilson, D.N. (登録日: 2015-03-31, 公開日: 2015-06-03, 最終更新日: 2025-03-19)

主引用文献

Polikanov, Y.S.,Starosta, A.L.,Juette, M.F.,Altman, R.B.,Terry, D.S.,Lu, W.,Burnett, B.J.,Dinos, G.,Reynolds, K.A.,Blanchard, S.C.,Steitz, T.A.,Wilson, D.N.
Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A.
Mol.Cell, 58:832-844, 2015

PubMed Abstract: The increase in multi-drug-resistant bacteria is limiting the effectiveness of currently approved antibiotics, leading to a renewed interest in antibiotics with distinct chemical scaffolds. We have solved the structures of the Thermus thermophilus 70S ribosome with A-, P-, and E-site tRNAs bound and in complex with either the aminocyclitol-containing antibiotic hygromycin A (HygA) or the nucleoside antibiotic A201A. Both antibiotics bind at the peptidyl transferase center and sterically occlude the CCA-end of the A-tRNA from entering the A site of the peptidyl transferase center. Single-molecule Förster resonance energy transfer (smFRET) experiments reveal that HygA and A201A specifically interfere with full accommodation of the A-tRNA, leading to the presence of tRNA accommodation intermediates and thereby inhibiting peptide bond formation. Thus, our results provide not only insight into the mechanism of action of HygA and A201A, but also into the fundamental process of tRNA accommodation during protein synthesis.

PubMed: 26028538
DOI: 10.1016/j.molcel.2015.04.014

実験手法

X-RAY DIFFRACTION (2.65 Å)