Fulltext

Structure and properties of the C-terminal β-helical domain of VgrG protein from Escherichia coli O157

Uchida, Kazuya ; Leiman, Petr G. ; Arisaka, Fumio ; Kanamaru, Shuji

In: The Journal of Biochemistry, 2014, vol. 155, no. 3, p. 173-182

Add to personal list
    Title
    • Structure and properties of the C-terminal β-helical domain of VgrG protein from Escherichia coli O157
    Author
    • Uchida, Kazuya. Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B9 Nagatsuta-cho, Midori-ku, Yokohama 226-8501 Japan; and École Polytechnique Fédérale de Lausanne (EPFL), Laboratory of Structural Biology and Biophysics, BSP-415, CH-1015 Lausanne, Switzerland
    • Leiman, Petr G.. Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B9 Nagatsuta-cho, Midori-ku, Yokohama 226-8501 Japan; and École Polytechnique Fédérale de Lausanne (EPFL), Laboratory of Structural Biology and Biophysics, BSP-415, CH-1015 Lausanne, Switzerland
    • Arisaka, Fumio. Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B9 Nagatsuta-cho, Midori-ku, Yokohama 226-8501 Japan; and École Polytechnique Fédérale de Lausanne (EPFL), Laboratory of Structural Biology and Biophysics, BSP-415, CH-1015 Lausanne, Switzerland
    • Kanamaru, Shuji. Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B9 Nagatsuta-cho, Midori-ku, Yokohama 226-8501 Japan; and École Polytechnique Fédérale de Lausanne (EPFL), Laboratory of Structural Biology and Biophysics, BSP-415, CH-1015 Lausanne, Switzerland
    Document Type
    • Postprint
    Language
    • English
    Published in
    • The Journal of Biochemistry, 2014, vol. 155, no. 3, p. 173-182. Oxford University Press
    Other Version
    OAI-PMH Identifier
    • oai:doc.rero.ch:299430
    Summary
    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. Valine-glycine repeat protein G (VgrG) proteins, which are the homologues of the gp27-gp5 (gene product) 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 β-structure. We also solved the crystal structure of a trypsin-resistant C-terminal fragment of E. coli O157 VgrG1 (VgrG1CG561) at 1.95 Å resolution. VgrG1CG561 forms a three-stranded antiparallel β-helix which is structurally similar to the β-helix domain of the central spike protein (gp138) of phi92 phage, indicating a possible evolutional relationship. Comparison of four different three-stranded β-helix proteins shows how their amino acid composition determines the protein fold