Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural Basis of the Immunity Mechanisms of Pediocin-like Bacteriocins.
Journal, issue, pages	Appl Environ Microbiol, Vol. 88, Issue 13, Page e0048122, Year 2022
Publish date	Jul 12, 2022
Authors	Liyan Zhu / Jianwei Zeng / Jiawei Wang /
PubMed Abstract	Pediocin-like bacteriocins, also designated class IIa bacteriocins, are ribosomally synthesized antimicrobial peptides targeting species closely related to the producers. They act on the cytoplasmic ...Pediocin-like bacteriocins, also designated class IIa bacteriocins, are ribosomally synthesized antimicrobial peptides targeting species closely related to the producers. They act on the cytoplasmic membrane of Gram-positive cells by dissipating the transmembrane electrical potential through pore formation with the mannose phosphotransferase system (man-PTS) as the target/receptor. Bacteriocin-producing strains also synthesize a cognate immunity protein that protects them against their own bacteriocins. Herein, we report the cryo-electron microscopy structure of the bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei. The complex structure reveals that pediocin-like bacteriocins bind to the same position on the Core domain of man-PTS, while the C-terminal helical tails of bacteriocins delimit the opening range of the Core domain away from the Vmotif domain to facilitate transmembrane pore formation. Upon attack of bacteriocins from the extracellular side, man-PTS exposes its cytosolic side for recognition of the N-terminal four-helix bundle of the immunity protein. The C-terminal loop of the immunity protein then inserts into the pore and blocks leakage induced by bacteriocins. Elucidation of the toxicity and immunity mechanisms of pediocin-like bacteriocins could support the design of novel bacteriocins against antibiotic-resistant pathogenic bacteria. Pediocin-like bacteriocins, ribosomally synthesized antimicrobial peptides, are generally co-expressed with cognate immunity proteins to protect the bacteriocin-producing strain from its own bacteriocin. Bacteriocins are considered potential alternatives to conventional antibiotics in the context of the bacterial resistance crisis, but the immunity mechanism is unclear. This study uncovered the mechanisms of action and immunity of class IIa bacteriocins.
External links	Appl Environ Microbiol / PubMed:35703550 / PubMed Central
Methods	EM (single particle)
Resolution	2.2 - 2.54 Å
Structure data	33321 7xno EMDB-33321, PDB-7xno: Cryo-EM structure of the bacteriocin-receptor-immunity ternary complex from Lactobacillus sakei Method: EM (single particle) / Resolution: 2.54 Å 33448 7xtg EMDB-33448, PDB-7xtg: Cryo-EM structure of Listeria monocytogenes man-PTS complexed with pediocin PA-1 Method: EM (single particle) / Resolution: 2.2 Å
Chemicals	ChemComp-MAN: alpha-D-mannopyranose
Source	latilactobacillus sakei l45 (bacteria) listeria monocytogenes (bacteria) pediococcus acidilactici (bacteria) latilactobacillus sakei (bacteria)
Keywords	MEMBRANE PROTEIN/IMMUNE SYSTEM / antimicrobial peptides / bacteriocins / pediocin-like/class IIa bacteriocins / antibiotic resistance / mannose phosphotransferase / man-PTS / immunity / self-protection / MEMBRANE PROTEIN / MEMBRANE PROTEIN-IMMUNE SYSTEM complex / Bacteriocin / PTS / ManYZ / ManY / ManZ / transporter / Mannose / PROTEIN TRANSPORT / Listeria monocytogenes / Pediococcus acidilactici / Latilactobacillus sakei / Mannose Phosphotransferase System