The bacterial type II secretion system is responsible for a wide range of infections, killing millions of people every year. The secretion system comprises a cytoplasmic ATPase, an inner-membrane platform, periplasmic domains, and an outer-membrane pore or secretin. Here, we are interested in the structure and dynamics of the pilus assembly components and signaling between periplasm where the secreted toxin is recognized and cytoplasm where the ATPase resides.
Rehman, S., Gu, S., Shevchik, V.E., Pickersgill, R.W. (2013) Anatomy of secretin-binding to the D. dadantii type II secretion system pilotin. Acta Crystallogr D Biol Crystallogr. 69, 1381-1386.
Wang, X., Pineau, C., Gu, S., Guschinskaya, N., Pickersgill, R.W., Shevchik, V.E. (2012) Cysteine scanning mutagenesis and disulfide mapping analysis of the arrangement of GspC and GspD protomers within the T2SS. J. Biol. Chem. 287, 19082-19093.
Gu, S., Kelly, G., Shevchik, V., Pickersgill, R.W. (2012) Solution structure of the HR domain and its interaction with the outer membrane secretin of the type II secretion system. J. Biol. Chem. 287, 9072-9080.
Gu, S., Rehman, S., Shevchik, V.E., Pickersgill, R.W. (2012) Structural and functional insights into the pilotin-secretin complex of the type II secretion system. PLOS Pathogens 8: e1002531.
Login, F., Fries, M., Pickersgill, R.W. & Shevchik, V. (2010) A 20-residue peptide of the inner membrane protein OutC mediates interaction with two distinct sites of the outer membrane secretin OutD and is essential for the functional type II secretion. Mol Micro. 76, 944-955.