Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme.
作者： Min Xu , Arockiasamy Arulandu , Douglas K Struck , Stephanie Swanson , James C Sacchettini
关键词: Hydrolase 、 Protein structure 、 Lysozyme 、 Bilayer 、 Periplasmic space 、 Isomerization 、 Lipid bilayer 、 Cysteine 、 Stereochemistry 、 Biology
摘要: The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic biochemical experiments show that, when released from bilayer, activated by intramolecular thiol-disulfide isomerization, which requires a cysteine its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm alternative disulfide linkages two forms reveal dramatic conformational differences catalytic Thus, exported endolysin kept three levels control-topological, conformational, covalent-until release membrane triggered holin.
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