9MNE

Crystal structure of enteropathogenic Escherichia coli EspC

This is a non-PDB format compatible entry.

Summary for 9MNE

• Entry DOI: 10.2210/pdb9mne/pdb
• Descriptor: Serine protease EspC, HEXAETHYLENE GLYCOL, 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL, ... (6 entities in total)
• Functional Keywords: autotransporter protein, serine protease, toxins, bacterial infections, secretion system, diarrhoea, hydrolase
• Biological source: Escherichia coli O127:H6
• Total number of polymer chains: 2
• Total formula weight: 212042.10

Authors

Pilapitiya, A.U.,Heras, B.,Paxman, J.J. (deposition date: 2024-12-21, release date: 2025-10-29)

Primary citation

Pilapitiya, A.U.,Hor, L.,Pan, J.,Wijeyewickrema, L.C.,Pike, R.N.,Leyton, D.L.,Paxman, J.J.,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, 17:2483777-2483777, 2025

PubMed Abstract: Enteropathogenic (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 (α) revealing a toxin comprised a serine protease attached to a large β-helix with additional subdomains. Using various modified EspC expression constructs, alongside type III secretion system-mediated cell internalization assays, we dissect how the α structural features enable toxin entry into the intestinal epithelium to cause cell cytotoxicity.

PubMed: 40164999
DOI: 10.1080/19490976.2025.2483777

Experimental method

X-RAY DIFFRACTION (2.94 Å)