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- Title
Structure of bacteriophage SPN1 S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity.
- Authors
Park, Yangshin; Lim, Jeong‐A.; Kong, Minsuk; Ryu, Sangryeol; Rhee, Sangkee
- Abstract
Bacteriophage SPN1 S infects the pathogenic Gram-negative bacterium S almonella typhimurium and expresses endolysin for the release of phage progeny by degrading peptidoglycan of the host cell walls. Bacteriophage SPN1 S endolysin exhibits high glycosidase activity against peptidoglycans, resulting in antimicrobial activity against a broad range of outer membrane-permeabilized Gram-negative bacteria. Here, we report a crystal structure of SPN1 S endolysin, indicating that unlike most endolysins from Gram-negative bacteria background, the α-helical protein consists of two modular domains, a large and a small domain, with a concave groove between them. Comparison with other structurally homologous glycoside hydrolases indicated a possible peptidoglycan binding site in the groove, and the presence of a catalytic dyad in the vicinity of the groove, one residue in a large domain and the other in a junction between the two domains. The catalytic dyad was further validated by antimicrobial activity assay against outer membrane-permeabilized E scherichia coli. The three-helix bundle in the small domain containing a novel class of sequence motif exhibited binding affinity against outer membrane-permeabilized E . coli and was therefore proposed as the peptidoglycan-binding domain. These structural and functional features suggest that endolysin from a Gram-negative bacterial background has peptidoglycan-binding activity and performs glycoside hydrolase activity through the catalytic dyad.
- Subjects
BACTERIOPHAGES; PEPTIDOGLYCANS; GLYCOSIDASES; CRYSTAL structure; GRAM-negative bacteria
- Publication
Molecular Microbiology, 2014, Vol 92, Issue 2, p316
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/mmi.12555