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9mne

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Crystal structure of enteropathogenic Escherichia coli EspC

Structural highlights

9mne is a 2 chain structure with sequence from Escherichia coli O127:H6 str. E2348/69. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.94Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ESPC_ECO27 Serine protease with enterotoxic and cytotoxic activities. Cleaves fodrin, but does not cause its redistribution within epithelial cells. The exact role of EspC in EPEC pathogenesis is still unknown.^[1]

Publication Abstract from PubMed

Enteropathogenic E. coli (EPEC) is a significant cause of diarrhea, leading to high infant mortality rates. A key toxin produced by EPEC is the EspC autotransporter, which is regulated alongside genes from the locus of enterocyte effacement (LEE), which collectively result in the characteristic attaching and effacing lesions on the intestinal epithelium. In this study, we present the crystal structure of the EspC passenger domain (alpha(EspC)) revealing a toxin comprised a serine protease attached to a large beta-helix with additional subdomains. Using various modified EspC expression constructs, alongside type III secretion system-mediated cell internalization assays, we dissect how the alpha(EspC) structural features enable toxin entry into the intestinal epithelium to cause cell cytotoxicity.

The crystal structure of the toxin EspC from enteropathogenic Escherichia coli reveals the mechanism that governs host cell entry and cytotoxicity.,Pilapitiya AU, Hor L, Pan J, Wijeyewickrema LC, Pike RN, Leyton DL, Paxman JJ, Heras B Gut Microbes. 2025 Dec;17(1):2483777. doi: 10.1080/19490976.2025.2483777. Epub , 2025 Mar 31. PMID:40164999^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Navarro-García F, Canizalez-Roman A, Sui BQ, Nataro JP, Azamar Y. The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E. coli. Infect Immun. 2004 Jun;72(6):3609-21. PMID:15155671 doi:10.1128/IAI.72.6.3609-3621.2004
↑ Pilapitiya AU, Hor L, Pan J, Wijeyewickrema LC, Pike RN, Leyton DL, Paxman JJ, Heras B. The crystal structure of the toxin EspC from enteropathogenic Escherichia coli reveals the mechanism that governs host cell entry and cytotoxicity. Gut Microbes. 2025 Dec;17(1):2483777. PMID:40164999 doi:10.1080/19490976.2025.2483777