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 Cited by 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: 33972673DOI: 10.1038/s42003-021-02068-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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