7VLX

Cryo-EM structures of Listeria monocytogenes man-PTS

7VLX の概要

• エントリーDOI: 10.2210/pdb7vlx/pdb
• EMDBエントリー: 32030
• 分子名称: Mannose/fructose/sorbose family PTS transporter subunit IIC, PTS mannose family transporter subunit IID, alpha-D-mannopyranose (3 entities in total)
• 機能のキーワード: antimicrobial peptides; bacteriocins; pediocin pa-1; pediocin-like/class iia bacteriocins; antibiotic resistance; mannose phosphotransferase; man-pts, membrane protein
• 由来する生物種: Listeria monocytogenes; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 182879.64

構造登録者

Wang, J.W. (登録日: 2021-10-05, 公開日: 2021-12-01, 最終更新日: 2025-06-18)

主引用文献

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

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: 34851716
DOI: 10.1128/AEM.01992-21

実験手法

ELECTRON MICROSCOPY (3.12 Å)