2HHH

Crystal structure of kasugamycin bound to the 30S ribosomal subunit

2HHH の概要

• エントリーDOI: 10.2210/pdb2hhh/pdb
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (22 entities in total)
• 機能のキーワード: ribosome, 30s, antibiotics, initiation
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 784440.75

構造登録者

Schluenzen, F. (登録日: 2006-06-28, 公開日: 2006-09-26, 最終更新日: 2024-04-03)

主引用文献

Schluenzen, F.,Takemoto, C.,Wilson, D.N.,Kaminishi, T.,Harms, J.M.,Hanawa-Suetsugu, K.,Szaflarski, W.,Kawazoe, M.,Shirouzo, M.,Nierhaus, K.H.,Yokoyama, S.,Fucini, P.
The antibiotic kasugamycin mimics mRNA nucleotides to destabilize tRNA binding and inhibit canonical translation initiation.
Nat.Struct.Mol.Biol., 13:871-878, 2006

PubMed Abstract: Kasugamycin (Ksg) specifically inhibits translation initiation of canonical but not of leaderless messenger RNAs. Ksg inhibition is thought to occur by direct competition with initiator transfer RNA. The 3.35-A structure of Ksg bound to the 30S ribosomal subunit presented here provides a structural description of two Ksg-binding sites as well as a basis for understanding Ksg resistance. Notably, neither binding position overlaps with P-site tRNA; instead, Ksg mimics codon nucleotides at the P and E sites by binding within the path of the mRNA. Coupled with biochemical experiments, our results suggest that Ksg indirectly inhibits P-site tRNA binding through perturbation of the mRNA-tRNA codon-anticodon interaction during 30S canonical initiation. In contrast, for 70S-type initiation on leaderless mRNA, the overlap between mRNA and Ksg is reduced and the binding of tRNA is further stabilized by the presence of the 50S subunit, minimizing Ksg efficacy.

PubMed: 16998488
DOI: 10.1038/nsmb1145

実験手法

X-RAY DIFFRACTION (3.35 Å)