The development of antibiotics has made it possible to cure many infections. Unfortunately, overuse of antibiotics has led to a rapid increase in antibiotic-resistant strains. Bacteriophage-encoded endolysins have emerged as a new class of antibacterial agents to combat surging antibiotic resistance. We were determined the structure of mtEC340M, which is an engineered endolysin EC340 of the PBEC131 phage that infects E. coli. The mtEC340M has 2.4 Å resolution diffraction data and consisting of 8 α-helices and 2 loops. The three active residues of mtEC340M were predicted by structural comparison with peptidoglycan-degrading lysozyme. LNT113 added cecropin A to the N-terminus to enhance antibacterial activity in the engineered mtEC340M.
<br>In this paper, the crystal structure of mtEC340M was identified and structural differences were confirmed by modeling LNT113. We would like to contribute to the development of Gram-negative bacteria-derived endolysin-based antibacterial agents based on structural differences between mtEC340M and LNT113.
