Structural highlights
Function
Q8XBV2_ECOLX The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. After endocytosis, the A subunit is cleaved by furin in two fragments, A1 and A2: A1 is the catalytically active fragment, and A2 is essential for holotoxin assembly with the B subunits.[ARBA:ARBA00043904]
Publication Abstract from PubMed
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 A 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.
Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin.,Watanabe-Takahashi M, Tamada M, Senda M, Hibino M, Shimizu E, Okuta A, Miyazawa A, Senda T, Nishikawa K Commun Biol. 2021 May 10;4(1):538. doi: 10.1038/s42003-021-02068-3. PMID:33972673[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 2021 May 10;4(1):538. PMID:33972673 doi:10.1038/s42003-021-02068-3
