6FKR

Crystal structure of the dolphin proline-rich antimicrobial peptide Tur1A bound to the Thermus thermophilus 70S ribosome

これはPDB形式変換不可エントリーです。

6FKR の概要

• エントリーDOI: 10.2210/pdb6fkr/pdb
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (58 entities in total)
• 機能のキーワード: antimicrobial peptide, antibiotic, inhibitor, ribosome
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 107
• 化学式量合計: 4356763.81

構造登録者

Mardirossian, M.,Perebaskine, N.,Benincasa, M.,Gambato, S.,Hofmann, S.,Huter, P.,Muller, C.,Hilpert, K.,Innis, C.A.,Tossi, A.,Wilson, D.N. (登録日: 2018-01-24, 公開日: 2018-03-28, 最終更新日: 2025-03-12)

主引用文献

Mardirossian, M.,Perebaskine, N.,Benincasa, M.,Gambato, S.,Hofmann, S.,Huter, P.,Muller, C.,Hilpert, K.,Innis, C.A.,Tossi, A.,Wilson, D.N.
The Dolphin Proline-Rich Antimicrobial Peptide Tur1A Inhibits Protein Synthesis by Targeting the Bacterial Ribosome.
Cell Chem Biol, 25:530-539.e7, 2018

PubMed Abstract: Proline-rich antimicrobial peptides (PrAMPs) internalize into susceptible bacteria using specific transporters and interfere with protein synthesis and folding. To date, mammalian PrAMPs have so far been identified only in artiodactyls. Since cetaceans are co-phyletic with artiodactyls, we mined the genome of the bottlenose dolphin Tursiops truncatus, leading to the identification of two PrAMPs, Tur1A and Tur1B. Tur1A, which is orthologous to the bovine PrAMP Bac7, is internalized into Escherichia coli, without damaging the membranes, using the inner membrane transporters SbmA and YjiL/MdM. Furthermore, like Bac7, Tur1A also inhibits bacterial protein synthesis by binding to the ribosome and blocking the transition from the initiation to the elongation phase. By contrast, Tur1B is a poor inhibitor of protein synthesis and may utilize another mechanism of action. An X-ray structure of Tur1A bound within the ribosomal exit tunnel provides a basis to develop these peptides as novel antimicrobial agents.

PubMed: 29526712
DOI: 10.1016/j.chembiol.2018.02.004

実験手法

X-RAY DIFFRACTION (3.2 Å)