7VLY
Cryo-EM structure of Listeria monocytogenes man-PTS complexed with pediocin PA-1
Summary for 7VLY
| Entry DOI | 10.2210/pdb7vly/pdb |
| EMDB information | 32030 32031 |
| Descriptor | Mannose/fructose/sorbose family PTS transporter subunit IIC, PTS mannose family transporter subunit IID, Bacteriocin pediocin PA-1, ... (5 entities in total) |
| Functional Keywords | antimicrobial peptides; bacteriocins; pediocin pa-1; pediocin-like/class iia bacteriocins; antibiotic resistance; mannose phosphotransferase; man-pts, membrane protein |
| Biological source | Listeria monocytogenes More |
| Total number of polymer chains | 9 |
| Total formula weight | 197884.64 |
| Authors | Wang, J.W. (deposition date: 2021-10-05, release date: 2021-12-01, Last modification date: 2025-07-02) |
| Primary citation | Zhu, L.,Zeng, J.,Wang, C.,Wang, J. Structural Basis of Pore Formation in the Mannose Phosphotransferase System by Pediocin PA-1. Appl.Environ.Microbiol., 88:e0199221-e0199221, 2022 Cited by PubMed Abstract: Bacteriocins are ribosomally synthesized bacterial antimicrobial peptides that have a narrow spectrum of antibacterial activity against species closely related to the producers. Pediocin-like (or class IIa) bacteriocins (PLBs) exhibit antibacterial activity against several Gram-positive bacterial strains by forming pores in the cytoplasmic membrane of target cells with a specific receptor, the mannose phosphotransferase system (man-PTS). In this study, we report the cryo-electron microscopy structures of man-PTS from Listeria monocytogenes alone and its complex with pediocin PA-1, the first and most extensively studied representative PLB, at resolutions of 3.12 and 2.45 Å, respectively. The structures revealed that the binding of pediocin PA-1 opens the Core domain of man-PTS away from its Vmotif domain, creating a pore through the cytoplasmic membranes of target cells. During this process, the N-terminal β-sheet region of pediocin PA-1 can specifically attach to the extracellular surface of the man-PTS Core domain, whereas the C-terminal half penetrates the membrane and cracks the man-PTS like a wedge. Thus, our findings shed light on a design of novel PLBs that can kill the target pathogenic bacteria. Listeria monocytogenes is a ubiquitous microorganism responsible for listeriosis, a rare but severe disease in humans, who become infected by ingesting contaminated food products (i.e., dairy, meat, fish, and vegetables): the disease has a fatality rate of 33%. Pediocin PA-1 is an important commercial additive used in food production to inhibit species. The mannose phosphotransferase system (man-PTS) is responsible for the sensitivity of Listeria monocytogenes to pediocin PA-1. In this study, we report the cryo-EM structures of man-PTS from Listeria monocytogenes alone and its complex with pediocin PA-1 at resolutions of 3.12 and 2.45 Å, respectively. Our results facilitate the understanding of the mode of action of class IIa bacteriocins as an alternative to antibiotics. PubMed: 34851716DOI: 10.1128/AEM.01992-21 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.45 Å) |
Structure validation
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