Dr. Long Li published a paper in PNAS with his collaborator.
The vast majority of secretory proteins in bacteria are translocated across the cell membranes through the SecY channel by a highly conserved ATPase, SecA. We report the structures of the active SecA–SecY with a moving protein substrate in both ADP (adenosine diphosphate) and ATP (adenosine triphosphate) states. The structures reveal that SecA moves protein substrates using an unexpected mechanism that is strikingly similar to how helicases move DNA/RNA substrates. Common structural features are shared by the active SecA–SecY complex and other protein translocation systems targeted by antibiotics, suggesting that SecA could be a highly potent target for antibiotic development against both gram-positive and gram-negative bacteria.
Original link: https://www.pnas.org/doi/10.1073/pnas.2208070120.
