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Solution Structure of Enterocin HF, an Antilisterial Bacteriocin Produced by Enterococcus faecium M3K31

Arbulu, Sara, Lohans, Christopher T., van Belkum, Marco J., Cintas, Luis M., Herrnaz, Carmen, Vederas, John C., Hernandez, Pablo E.
Journal of agricultural and food chemistry 2015 v.63 no.49 pp. 10689-10695
Enterococcus faecium, amino acids, antibacterial properties, bacteriocins, mechanism of action, nuclear magnetic resonance spectroscopy
The solution structure of enterocin HF (EntHF), a class IIa bacteriocin of 43 amino acids produced by Enterococcus faecium M3K31, was evaluated by CD and NMR spectroscopy. Purified EntHF was unstructured in water, but CD analysis supports that EntHF adopts an α-helical conformation when exposed to increasing concentrations of trifluoroethanol. Furthermore, NMR spectroscopy indicates that this bacteriocin adopts an antiparallel β-sheet structure in the N-terminal region (residues 1–17), followed by a well-defined central α-helix (residues 19–30) and a more disordered C-terminal end (residues 31–43). EntHF could be structurally organized into three flexible regions that might act in a coordinated manner. This is in agreement with the absence of long-range nuclear Overhauser effect signals between the β-sheet domain and the C-terminal end of the bacteriocin. The 3D structure recorded for EntHF fits emerging facts regarding target recognition and mode of action of class IIa bacteriocins.