4IJY

Crystal Structure of the ETEC Secreted Protein CofJ

Summary for 4IJY

• Entry DOI: 10.2210/pdb4ijy/pdb
• Descriptor: CofJ, IODIDE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: beta-sandwich, secreted protein, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 38675.80

Authors

Craig, L.,Kolappan, S.,Yuen, A.S.W. (deposition date: 2012-12-24, release date: 2013-10-16, Last modification date: 2024-11-20)

Primary citation

Yuen, A.S.,Kolappan, S.,Ng, D.,Craig, L.
Structure and secretion of CofJ, a putative colonization factor of enterotoxigenic Escherichia coli.
Mol.Microbiol., 90:898-918, 2013

PubMed Abstract: Enterotoxigenic Escherichia coli (ETEC) colonize the human gut, causing severe cholera-like diarrhoea. ETEC utilize a diverse array of pili and fimbriae for host colonization, including the Type IVb pilus CFA/III. The CFA/III pilus machinery is encoded on the cof operon, which is similar in gene sequence and synteny to the tcp operon that encodes another Type IVb pilus, the Vibrio cholerae toxin co-regulated pilus (TCP). Both pilus operons possess a syntenic gene encoding a protein of unknown function. In V. cholerae, this protein, TcpF, is a critical colonization factor secreted by the TCP apparatus. Here we show that the corresponding ETEC protein, CofJ, is a soluble protein secreted via the CFA/III apparatus. We present a 2.6 Å resolution crystal structure of CofJ, revealing a large β-sandwich protein that bears no sequence or structural homology to TcpF. CofJ has a cluster of exposed hydrophobic side-chains at one end and structural homology to the pore-forming proteins perfringolysin O and α-haemolysin. CofJ binds to lipid vesicles and epithelial cells, suggesting a role in membrane attachment during ETEC colonization.

PubMed: 24106767
DOI: 10.1111/mmi.12407

Experimental method

X-RAY DIFFRACTION (2.6 Å)