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Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement (2013)
Journal Article
Vankemmelbeke, M., Housden, N. G., James, R., Kleanthous, C., & Penfold, C. N. (2013). Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement. Microbiology Open, 2(5), https://doi.org/10.1002/mbo3.122

Nuclease colicins bind their target receptor BtuB in the outer membrane of sensitive Escherichia coli cells in the form of a high-affinity complex with their cognate immunity proteins. The release of the immunity protein from the colicin complex is a... Read More about Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement.

Structural evidence that colicin a protein binds to a novel binding site of TolA protein in Escherichia coli periplasm (2012)
Journal Article
Li, C., Zhang, Y., Vankemmelbeke, M., Hecht, O., Aleanizy, F. S., Macdonald, C., …Penfold, C. N. (2012). Structural evidence that colicin a protein binds to a novel binding site of TolA protein in Escherichia coli periplasm. Journal of Biological Chemistry, 287(23), https://doi.org/10.1074/jbc.M112.342246

The Tol assembly of proteins is an interacting network of proteins located in the Escherichia coli cell envelope that transduces energy and contributes to cell integrity. TolA is central to this network linking the inner and outer membranes by intera... Read More about Structural evidence that colicin a protein binds to a novel binding site of TolA protein in Escherichia coli periplasm.