Structural basis for MurJ inhibition by phage lysis protein Sgl PP7 suggesting convergence

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Abstract

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, Sgl PP7 . MurJ was locked in an outward-facing conformation by Sgl PP7 , similar to the MurJ/Lys M complex; however, distinct interactions suggest convergent evolution among phage lysis proteins.

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