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Science 7 January 2005:
Vol. 307. no. 5706, pp. 113 - 117
DOI: 10.1126/science.1105143
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Reports

Disulfide Isomerization After Membrane Release of Its SAR Domain Activates P1 Lysozyme

Min Xu,* Arockiasamy Arulandu,* Douglas K. Struck, Stephanie Swanson, James C. Sacchettini,{dagger} Ry Young{dagger}

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.

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843–2128, USA.



* These authors contributed equally to the results described in this work.

{dagger} To whom correspondence should be addressed. E-mail: sacchett{at}tamu.edu (J.C.S.) and ryland{at}tamu.edu (R.Y.).

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