bioRxivJClub
Structural Basis for Dual Peptidoglycan Hydrolysis by an E. faecium Minhovirus Tail Spike Lysin
bioRxiv · · Preprint · Open access
MESNAGE, Wilson + 8 more
Abstract ↗AI summary
The abstract is read at the publisher; the summary is JClub's.
ORF11 from the Enterococcus faecium Minhovirus SHEF14 tail-spike lysin shows a 2.5 Angstrom crystal structure with four domains enabling dual peptidoglycan hydrolysis.
- Why it matters: Phages must breach bacterial cell walls to infect, but the structural basis for how Enterococcus podoviruses perform peptidoglycan cleavage is not well defined.
- What they did: The authors solved the ORF11 2.5 Angstrom structure, identified domain organization (D1 glycosyl hydrolase, D4 CHAP, D2 helical linker, D3 CHAP-like), and used recombinant protein plus LC-MS/MS.
- The result: ORF11 is confirmed to act as both an N-acetylglucosaminidase and a D,D-endopeptidase, cleaving the D-alanine4–D-aspartate bond, providing the first structural description of an Enterococcus podovirus tail-spike lysin.
The findingWhy it mattersWhat they didThe result
- Open access