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7d6q

From Proteopedia

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Current revision

Crystal structure of the Stx2a

Structural highlights

7d6q is a 6 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7d6q"

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 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/Q8XBV2_ECOLX Q8XBV2_ECOLX]
+[https://www.uniprot.org/uniprot/Q8XBV2_ECOLX 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]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

7d6q

From Proteopedia

Current revision

Crystal structure of the Stx2a

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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