5HCP

Crystal structure of antimicrobial peptide Metalnikowin bound to the Thermus thermophilus 70S ribosome

これはPDB形式変換不可エントリーです。

5HCP の概要

• エントリーDOI: 10.2210/pdb5hcp/pdb
• 関連するPDBエントリー: 5HAU 5HCQ 5HCR 5HD1
• 分子名称: 23S Ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (59 entities in total)
• 機能のキーワード: metalnikowin, antimicrobial peptide, antibiotic, 70s ribosome, inhibition of translation, peptidyl transferase inhibitors, 50s ribosomal subunit, peptide exit tunnel, 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: 110
• 化学式量合計: 4466943.38

構造登録者

Gagnon, M.G.,Roy, R.N.,Lomakin, I.B.,Florin, T.,Mankin, A.S.,Steitz, T.A. (登録日: 2016-01-04, 公開日: 2016-04-06, 最終更新日: 2024-03-06)

主引用文献

Gagnon, M.G.,Roy, R.N.,Lomakin, I.B.,Florin, T.,Mankin, A.S.,Steitz, T.A.
Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition.
Nucleic Acids Res., 44:2439-2450, 2016

PubMed Abstract: With bacterial resistance becoming a serious threat to global public health, antimicrobial peptides (AMPs) have become a promising area of focus in antibiotic research. AMPs are derived from a diverse range of species, from prokaryotes to humans, with a mechanism of action that often involves disruption of the bacterial cell membrane. Proline-rich antimicrobial peptides (PrAMPs) are instead actively transported inside the bacterial cell where they bind and inactivate specific targets. Recently, it was reported that some PrAMPs, such as Bac71 -35, oncocins and apidaecins, bind and inactivate the bacterial ribosome. Here we report the crystal structures of Bac71 -35, Pyrrhocoricin, Metalnikowin and two oncocin derivatives, bound to the Thermus thermophilus 70S ribosome. Each of the PrAMPs blocks the peptide exit tunnel of the ribosome by simultaneously occupying three well characterized antibiotic-binding sites and interferes with the initiation step of translation, thereby revealing a common mechanism of action used by these PrAMPs to inactivate protein synthesis. Our study expands the repertoire of PrAMPs and provides a framework for designing new-generation therapeutics.

PubMed: 26809677
DOI: 10.1093/nar/gkw018

実験手法

X-RAY DIFFRACTION (2.894 Å)