6EPI

Structure of the epsilon_1 / zeta_1 antitoxin / toxin system from Neisseria gonorrhoeae in complex with UNAM-4P.

6EPI の概要

• エントリーDOI: 10.2210/pdb6epi/pdb
• 分子名称: Epsilon_1 antitoxin, Zeta_1 toxin, UDP-N-acetyl-muramic acid-4'phosphate, ... (6 entities in total)
• 機能のキーワード: bacterial toxin antitoxin systems, small molecule kinases, toxin
• 由来する生物種: Neisseria gonorrhoeae; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 212275.08

構造登録者

Rocker, A.,Meinhart, A. (登録日: 2017-10-11, 公開日: 2018-05-02, 最終更新日: 2024-01-17)

主引用文献

Rocker, A.,Peschke, M.,Kittila, T.,Sakson, R.,Brieke, C.,Meinhart, A.
The ng_ zeta 1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis.
Nat Commun, 9:1686-1686, 2018

PubMed Abstract: Bacterial toxin-antitoxin complexes are emerging as key players modulating bacterial physiology as activation of toxins induces stasis or programmed cell death by interference with vital cellular processes. Zeta toxins, which are prevalent in many bacterial genomes, were shown to interfere with cell wall formation by perturbing peptidoglycan synthesis in Gram-positive bacteria. Here, we characterize the epsilon/zeta toxin-antitoxin (TA) homologue from the Gram-negative pathogen Neisseria gonorrhoeae termed ng_ɛ1 / ng_ζ1. Contrary to previously studied streptococcal epsilon/zeta TA systems, ng_ɛ1 has an epsilon-unrelated fold and ng_ζ1 displays broader substrate specificity and phosphorylates multiple UDP-activated sugars that are precursors of peptidoglycan and lipopolysaccharide synthesis. Moreover, the phosphorylation site is different from the streptococcal zeta toxins, resulting in a different interference with cell wall synthesis. This difference most likely reflects adaptation to the individual cell wall composition of Gram-negative and Gram-positive organisms but also the distinct involvement of cell wall components in virulence.

PubMed: 29703974
DOI: 10.1038/s41467-018-03652-8

実験手法

X-RAY DIFFRACTION (2.8 Å)