4ZER

Crystal structure of the Onc112 antimicrobial peptide bound to the Thermus thermophilus 70S ribosome

これはPDB形式変換不可エントリーです。

4ZER の概要

• エントリーDOI: 10.2210/pdb4zer/pdb
• 分子名称: 23s ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (63 entities in total)
• 機能のキーワード: bacterial ribosome, proline-rich antimicrobial peptide, antibiotics, protein biosynthesis, ribosome
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 110
• 化学式量合計: 4412861.84

構造登録者

Seefeldt, A.C.,Nguyen, F.,Antunes, S.,Perebaskine, N.,Graf, M.,Arenz, S.,Inampudi, K.K.,Douat, C.,Guichard, G.,Wilson, D.N.,Innis, C.A. (登録日: 2015-04-20, 公開日: 2015-05-20, 最終更新日: 2025-03-12)

主引用文献

Seefeldt, A.C.,Nguyen, F.,Antunes, S.,Perebaskine, N.,Graf, M.,Arenz, S.,Inampudi, K.K.,Douat, C.,Guichard, G.,Wilson, D.N.,Innis, C.A.
The proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complex.
Nat.Struct.Mol.Biol., 22:470-475, 2015

PubMed Abstract: The increasing prevalence of multidrug-resistant pathogenic bacteria is making current antibiotics obsolete. Proline-rich antimicrobial peptides (PrAMPs) display potent activity against Gram-negative bacteria and thus represent an avenue for antibiotic development. PrAMPs from the oncocin family interact with the ribosome to inhibit translation, but their mode of action has remained unclear. Here we have determined a structure of the Onc112 peptide in complex with the Thermus thermophilus 70S ribosome at a resolution of 3.1 Å by X-ray crystallography. The Onc112 peptide binds within the ribosomal exit tunnel and extends toward the peptidyl transferase center, where it overlaps with the binding site for an aminoacyl-tRNA. We show biochemically that the binding of Onc112 blocks and destabilizes the initiation complex, thus preventing entry into the elongation phase. Our findings provide a basis for the future development of this class of potent antimicrobial agents.

PubMed: 25984971
DOI: 10.1038/nsmb.3034

実験手法

X-RAY DIFFRACTION (3.1 Å)