Journal
SCIENCE
Volume 307, Issue 5706, Pages 113-117Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1105143
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Funding
- NIGMS NIH HHS [R01 GM027099, GM27099, GM62410] Funding Source: Medline
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The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membra ne-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.
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