Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding.To escape from hosts after completing their life cycle, bacteriophages often use endolysins, which degrade bacterial peptidoglycan.  While mesophilic phages have been extensively studied, their thermophilic counterparts are not well characterized.  Here, we present a detailed analysis of the structure and function of Ts2631 endolysin from thermophilic phage vB_Tsc2631, which is a zinc-dependent amidase.  Because Ts2631 exhibits intrinsic antibacterial activity and unusual thermal stability, it is perfectly suited as a scaffold for the development of antimicrobial agents.
THERM