Related Experiment Video
Updated: Oct 29, 2026

A Fluorescence-based Assay of Phospholipid Scramblase Activity
Published on: September 20, 2016
Structural basis for inhibition of the lipid flippase MurJ by phage lysis protein SglPP7 suggests convergent
Kaito Hosoda1, Hidetaka Kohga1, Sixian Wu1
1Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Abstract:
Some bacteriophages encode lysis proteins that inhibit essential bacterial processes, and elucidating their mechanisms is valuable for developing antibacterial strategies against drug-resistant pathogens. We determined the cryo-EM structure of the complex between the essential Escherichia coli lipid II flippase MurJ and the phage lysis protein SglPP7. Structural, mutational, and molecular dynamics (MD) simulation analyses revealed that SglPP7 binds along the intramembrane cleft of MurJ and inserts its C-terminal tail into the internal cavity, stabilizing MurJ in an outward-facing conformation. Structural comparison with LysM (SglM) and SglCJ3 showed that these sequence-divergent Sgl proteins stabilize MurJ in the outward-facing conformation through distinct binding modes, consistent with the possibility of convergent evolution toward MurJ inhibition.
Related Concept Videos
Membrane Asymmetry Regulating Transporters
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
IP3/DAG Signaling Pathway
Pinching-off of Coated Vesicles
Regulation of Bacterial Virulence
Inhibitors of Bacterial Protein Synthesis

