Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. uri icon

abstract

  • The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of control-topological, conformational, and covalent-until its release from the membrane is triggered by the P1 holin.

published proceedings

  • Science

altmetric score

  • 4

author list (cited authors)

  • Xu, M., Arulandu, A., Struck, D. K., Swanson, S., Sacchettini, J. C., & Young, R. y.

citation count

  • 103

complete list of authors

  • Xu, Min||Arulandu, Arockiasamy||Struck, Douglas K||Swanson, Stephanie||Sacchettini, James C||Young, Ry

publication date

  • January 2005