Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme.
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Academic Article
individual record
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.
authors
publication outlet
Science
author list (cited authors)
Xu, M., Arulandu, A., Struck, D. K., Swanson, S., Sacchettini, J. C., & Young, R. y.
publication date
2005
publisher
keywords
- Enzyme Activation
- Chemical Phenomena
- Cell Membrane
- Crystallography, X-Ray
- Binding Sites
- Protein Sorting Signals
- Recombinant Fusion Proteins
- Isomerism
- Catalytic Domain
- Amino Acid Sequence
- Escherichia Coli
- Muramidase
- Bacteriophage P1
- Protein Structure, Secondary
- Protein Conformation
- Cysteine
- Molecular Sequence Data
- Protein Structure, Tertiary
- Lipid Bilayers
- Models, Molecular
- Chemistry, Physical
- Mutation
altmetric score
4.0
citation count
103