The glycocins: in a class of their own.
First reported in 2011, glycocins (glycosylated bacteriocins) are bacterial toxins that constitute a subset of ribosomally synthesised and post-translationally modified peptide (RiPP) natural products. Three NMR structures (glycocin F, ASM1 and sublancin 168), two with helix-loop-helix Cs α/α folds, are deposited in the PDB. Each structure contains a monosaccharide β-S-linked to a cysteine side chain. Three more glycocins (thurandacin, and enterocins F4-9 and 96) have been biochemically characterised, and others predicted on the basis of bioinformatic analyses. Only glycocin F, ASM1 and enterocin F4-9 are unequivocally glycoactive. This review probes the structure-function relationships of four types of nested disulfide-bonded glycocins.
Institute of Fundamental Sciences, College of Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. Electronic address: g.norris@massey.ac.nz.
Gillian E
GE
Norris
Institute of Fundamental Sciences, College of Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. Electronic address: m.l.patchett@massey.ac.nz.
Mark L
ML
Patchett
D001430:Bacteriocins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation
D001430:Bacteriocins