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
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Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for the extended-spectrum antimicrobial activity of Garvieacin Q.
Journal, issue, pages	Appl Environ Microbiol, Page e0177325, Year 2026
Publish date	Jan 21, 2026
Authors	Jinsong Duan / Dan Li / Yuqing Zhao / Jiawei Wang /
PubMed Abstract	Class IIa and IId bacteriocins are antimicrobial peptides with potential for combating antibiotic-resistant pathogens. However, their species-specific activity, dictated by recognition of the mannose ...Class IIa and IId bacteriocins are antimicrobial peptides with potential for combating antibiotic-resistant pathogens. However, their species-specific activity, dictated by recognition of the mannose phosphotransferase system (Man-PTS) receptor, often restricts their spectrum. Garvieacin Q/Garvicin Q (GarQ), a newly identified class IId bacteriocin, is unusual in that it targets both and the non-lactococcal pathogen , yet the structural basis for this cross-species activity has remained unclear. Using cryo-electron microscopy, we determined the structures of GarQ bound to Man-PTS receptors from and . In , the receptor contains a unique Tudor-like γ+ domain that sterically constrains the N terminus of incoming bacteriocins, thereby enforcing specificity for GarQ while excluding others such as lactococcin A (LcnA). In , GarQ engages the receptor through the same conserved binding mode, effectively bypassing the unusual species barrier. We further demonstrate that the C-terminal length of GarQ is a critical determinant of pore size and target specificity. Together, these findings uncover the structural mechanism underlying GarQ's atypical extended-spectrum activity and provide a framework for engineering bacteriocins with customized spectra to combat specific pathogens.IMPORTANCEThis study establishes a structural basis for how the extended-spectrum bacteriocin Garvieacin Q (GarQ) circumvents the canonical species-specificity of class II bacteriocins by engaging mannose phosphotransferase system receptors from different bacterial genera through both conserved and divergent binding modes. We identify a previously unknown Tudor-like γ+ domain in the receptor that sterically restricts the access of other bacteriocins, thereby defining bacteriocin specificity. Moreover, we demonstrate that the C-terminal length of GarQ critically determines pore size and bacterial targets, revealing an engineerable principle for designing synthetic bacteriocins with customized spectra against clinically relevant pathogens.
External links	Appl Environ Microbiol / PubMed:41562606
Methods	EM (single particle)
Resolution	2.87 - 3.81 Å
Structure data	66027 9wjr EMDB-66027, PDB-9wjr: Cryo-EM structure of the L. garvieae Man-PTS Method: EM (single particle) / Resolution: 2.87 Å 66030 9wju EMDB-66030, PDB-9wju: Cryo-EM structure of the L. garvieae Man-PTS in complex with the bacteriocin GarQ Method: EM (single particle) / Resolution: 3.81 Å 66032 9wjw EMDB-66032, PDB-9wjw: Cryo-EM structure of the GarQ-lmYZ complex Method: EM (single particle) / Resolution: 2.96 Å
Chemicals	ChemComp-MAN: alpha-D-mannopyranose
Source	lactococcus garvieae (lactic acid bacteria) listeria monocytogenes (bacteria)
Keywords	MEMBRANE PROTEIN / antibiotic resistance; antimicrobial peptides; mannose phosphotransferase system; Man-PTS; bacteriocins; non-pediocin-like/class IId bacteriocins; Garvicin Q; GarQ