Structural highlights
Function
[LYS_BPP21] Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Acts as a transglycosylase.
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
R(21), the lysozyme of coliphage 21, has an N-terminal signal-anchor-release (SAR) domain that directs its secretion in a membrane-tethered, inactive form and then its release and activation in the periplasm. Both genetic and crystallographic studies show that the SAR domain, once extracted from the bilayer, refolds into the body of the enzyme and effects muralytic activation by repositioning one residue of the canonical lysozyme catalytic triad.
Regulation of a muralytic enzyme by dynamic membrane topology.,Sun Q, Kuty GF, Arockiasamy A, Xu M, Young R, Sacchettini JC Nat Struct Mol Biol. 2009 Nov;16(11):1192-4. Epub 2009 Nov 1. PMID:19881499[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sun Q, Kuty GF, Arockiasamy A, Xu M, Young R, Sacchettini JC. Regulation of a muralytic enzyme by dynamic membrane topology. Nat Struct Mol Biol. 2009 Nov;16(11):1192-4. Epub 2009 Nov 1. PMID:19881499 doi:10.1038/nsmb.1681
