7D6Q

Crystal structure of the Stx2a

7D6Q の概要

• エントリーDOI: 10.2210/pdb7d6q/pdb
• 分子名称: rRNA N-glycosylase, Shiga toxin 2 B subunit, 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE, ... (4 entities in total)
• 機能のキーワード: shiga toxin, toxin
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 73156.14

構造登録者

Takahashi, M.,Tamada, M.,Hibino, M.,Senda, M.,Okuda, A.,Miyazawa, A.,Senda, T.,Nishikawa, K. (登録日: 2020-10-01, 公開日: 2021-04-14, 最終更新日: 2024-11-06)

主引用文献

Watanabe-Takahashi, M.,Tamada, M.,Senda, M.,Hibino, M.,Shimizu, E.,Okuta, A.,Miyazawa, A.,Senda, T.,Nishikawa, K.
Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin.
Commun Biol, 4:538-538, 2021

PubMed Abstract: Shiga toxin (Stx) is a major virulence factor of enterohemorrhagic Escherichia coli, which causes fatal systemic complications. Here, we identified a tetravalent peptide that inhibited Stx by targeting its receptor-binding, B-subunit pentamer through a multivalent interaction. A monomeric peptide with the same motif, however, did not bind to the B-subunit pentamer. Instead, the monomer inhibited cytotoxicity with remarkable potency by binding to the catalytic A-subunit. An X-ray crystal structure analysis to 1.6 Å resolution revealed that the monomeric peptide fully occupied the catalytic cavity, interacting with Glu167 and Arg170, both of which are essential for catalytic activity. Thus, the peptide motif demonstrated potent inhibition of two functionally distinct subunits of Stx.

PubMed: 33972673
DOI: 10.1038/s42003-021-02068-3

実験手法

X-RAY DIFFRACTION (1.8 Å)