4V9C

Allosteric control of the ribosome by small-molecule antibiotics

これはPDB形式変換不可エントリーです。

4V9C の概要

• エントリーDOI: 10.2210/pdb4v9c/pdb
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total)
• 機能のキーワード: nucleic acid conformation, protein biosynthesis, antibiotic, neomycin, aminoglycoside, rrf, recycling, ribosome-antibiotic complex, ribosome/antibiotic
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm:
• タンパク質・核酸の鎖数: 109
• 化学式量合計: 4402452.12

構造登録者

Cate, J.H.D.,Pulk, A.,Blanchard, S.C.,Wang, L.,Feldman, M.B.,Wasserman, M.R.,Altman, R. (登録日: 2012-07-25, 公開日: 2014-07-09, 最終更新日: 2024-10-30)

主引用文献

Wang, L.,Pulk, A.,Wasserman, M.R.,Feldman, M.B.,Altman, R.B.,Doudna Cate, J.H.,Blanchard, S.C.
Allosteric control of the ribosome by small-molecule antibiotics.
Nat.Struct.Mol.Biol., 19:957-963, 2012

PubMed Abstract: Protein synthesis is targeted by numerous, chemically distinct antibiotics that bind and inhibit key functional centers of the ribosome. Using single-molecule imaging and X-ray crystallography, we show that the aminoglycoside neomycin blocks aminoacyl-transfer RNA (aa-tRNA) selection and translocation as well as ribosome recycling by binding to helix 69 (H69) of 23S ribosomal RNA within the large subunit of the Escherichia coli ribosome. There, neomycin prevents the remodeling of intersubunit bridges that normally accompanies the process of subunit rotation to stabilize a partially rotated ribosome configuration in which peptidyl (P)-site tRNA is constrained in a previously unidentified hybrid position. Direct measurements show that this neomycin-stabilized intermediate is incompatible with the translation factor binding that is required for distinct protein synthesis reactions. These findings reveal the functional importance of reversible intersubunit rotation to the translation mechanism and shed new light on the allosteric control of ribosome functions by small-molecule antibiotics.

PubMed: 22902368
DOI: 10.1038/nsmb.2360

実験手法

X-RAY DIFFRACTION (3.3 Å)