7D6R

Crystal structure of the Stx2a complexed with MMA betaAla peptide

Summary for 7D6R

• Entry DOI: 10.2210/pdb7d6r/pdb
• Descriptor: rRNA N-glycosylase, Shiga toxin 2 B subunit, MMA betaAla peptide, ... (5 entities in total)
• Functional Keywords: shiga toxin, toxin
• Biological source: Escherichia coli; More
• Total number of polymer chains: 7
• Total formula weight: 74407.76

Authors

Takahashi, M.,Tamada, M.,Hibino, M.,Senda, M.,Okuda, A.,Miyazawa, A.,Senda, T.,Nishikawa, K. (deposition date: 2020-10-01, release date: 2021-04-14, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)