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Publication Abstract from PubMed

The bacterial Type 6 secretion system (T6SS) translocates protein toxins (also called effectors) from the cytosol of a T6SS-carrying cell to a target cell by a syringe-like supramolecular complex resembling a contractile tail of bacteriophages. VgrG proteins, which are the homologs of the gp27-gp5 cell puncturing complex of bacteriophage T4, are considered to be located at the attacking tip of the bacterial T6SS apparatus. Here, we over-expressed six VgrG proteins from pathogenic Escherichia coli O157 and CFT073 strains. Purified VgrG1 of E. coli O157 and c3393 of E. coli CFT073 form trimer in solution and are rich in beta-structure. We also solved the crystal structure of a trypsin-resistant C-terminal fragment of E. coli O157 VgrG1 (VgrG1CG561) at 1.95A resolution. VgrG1CG561 forms a three-stranded antiparallel beta-helix which is structurally similar to the beta-helix domain of the central spike protein (gp138) of phi92 phage, indicating a possible evolutional relationship. Comparison of four different three-stranded beta-helix proteins shows how their amino acid composition determines the protein fold.

Structure and properties of the C-terminal beta-helical domain of VgrG protein from Escherichia coli O157.,Uchida K, Leiman PG, Arisaka F, Kanamaru S J Biochem. 2013 Dec 3. PMID:24307403^[1]

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