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1FJG

STRUCTURE OF THE THERMUS THERMOPHILUS 30S RIBOSOMAL SUBUNIT IN COMPLEX WITH THE ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN, AND PAROMOMYCIN

1FJG の概要
エントリーDOI10.2210/pdb1fjg/pdb
関連するPDBエントリー1FJF 1QD7
分子名称16S RIBOSOMAL RNA, 30S RIBOSOMAL PROTEIN S9, 30S RIBOSOMAL PROTEIN S10, ... (27 entities in total)
機能のキーワード30s ribosomal subunit, ribosome, antibiotic, streptomycin, spectinomycin, paromomycin
由来する生物種Thermus thermophilus
詳細
タンパク質・核酸の鎖数22
化学式量合計789321.51
構造登録者
Carter, A.P.,Clemons Jr., W.M.,Brodersen, D.E.,Wimberly, B.T.,Morgan-Warren, R.J.,Ramakrishnan, V. (登録日: 2000-08-08, 公開日: 2000-09-25, 最終更新日: 2024-10-23)
主引用文献Carter, A.P.,Clemons Jr., W.M.,Brodersen, D.E.,Morgan-Warren, R.J.,Wimberly, B.T.,Ramakrishnan, V.
Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
Nature, 407:340-348, 2000
Cited by
PubMed Abstract: The 30S ribosomal subunit has two primary functions in protein synthesis. It discriminates against aminoacyl transfer RNAs that do not match the codon of messenger RNA, thereby ensuring accuracy in translation of the genetic message in a process called decoding. Also, it works with the 50S subunit to move the tRNAs and associated mRNA by precisely one codon, in a process called translocation. Here we describe the functional implications of the high-resolution 30S crystal structure presented in the accompanying paper, and infer details of the interactions between the 30S subunit and its tRNA and mRNA ligands. We also describe the crystal structure of the 30S subunit complexed with the antibiotics paromomycin, streptomycin and spectinomycin, which interfere with decoding and translocation. This work reveals the structural basis for the action of these antibiotics, and leads to a model for the role of the universally conserved 16S RNA residues A1492 and A1493 in the decoding process.
PubMed: 11014183
DOI: 10.1038/35030019
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 1fjg
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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