Structural highlights
Publication Abstract from PubMed
Endolysins produced by bacteriophages play essential roles in the release of phage progeny by degrading the peptidoglycan layers of the bacterial cell wall. Bacteriophage-encoded endolysins have emerged as a new class of antibacterial agents to combat surging antibiotic resistance. The crystal structure of mtEC340M, an engineered endolysin EC340 from the PBEC131 phage that infects Escherichia coli, was determined. The crystal structure of mtEC340M at 2.4 A resolution consists of eight alpha-helices and two loops. The three active residues of mtEC340M were predicted by structural comparison with peptidoglycan-degrading lysozyme.
Crystal structure of the engineered endolysin mtEC340M.,Wang JM, Seok SH, Yoon WS, Kim JH, Seo MD Acta Crystallogr F Struct Biol Commun. 2023 May 1;79(Pt 5):105-110. doi: , 10.1107/S2053230X23002583. Epub 2023 May 3. PMID:37132476[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang JM, Seok SH, Yoon WS, Kim JH, Seo MD. Crystal structure of the engineered endolysin mtEC340M. Acta Crystallogr F Struct Biol Commun. 2023 May 1;79(Pt 5):105-110. PMID:37132476 doi:10.1107/S2053230X23002583
