Structural basis for MurJ inhibition by phage lysis protein SglPP7 suggesting convergence
Hosoda, K.; Kohga, H.; Wu, S.; Tanaka, H.; Shigematsu, H.; Miyazaki, R.; Tsukazaki, T.
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Some bacteriophages encode lysis proteins that inhibit essential bacterial processes, the elucidation of which is valuable for developing antibacterial strategies against drug-resistant pathogens. We determined the cryo-EM structure of the complex between the essential E. coli lipid II flippase MurJ and a phage lysis protein, SglPP7. MurJ was locked in an outward-facing conformation by SglPP7, similar to the MurJ/LysM complex; however, distinct interactions suggest convergent evolution among phage lysis proteins.
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