Structural highlights
Function
ENLYS_BPP21 Signal-arrest-release (SAR) endolysin with lysozyme activity that degrades host peptidoglycans and participates with the pinholin and spanin proteins in the sequential events which lead to programmed host cell lysis releasing the mature viral particles. Once the pinholin has permeabilized the host cell membrane, the SAR-endolysin is released into the periplasm where it breaks down the peptidoglycan layer.[HAMAP-Rule:MF_04136]
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
