Structural highlights
Function
[LYS_BPP1] Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme.,Xu M, Arulandu A, Struck DK, Swanson S, Sacchettini JC, Young R Science. 2005 Jan 7;307(5706):113-7. PMID:15637279[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xu M, Arulandu A, Struck DK, Swanson S, Sacchettini JC, Young R. Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science. 2005 Jan 7;307(5706):113-7. PMID:15637279 doi:307/5706/113
