The glycocins: in a class of their own

Gillian E Norris; Mark L Patchett

doi:10.1016/j.sbi.2016.09.003

The glycocins: in a class of their own

Curr Opin Struct Biol. 2016 Oct:40:112-119. doi: 10.1016/j.sbi.2016.09.003. Epub 2016 Sep 21.

Authors

Gillian E Norris¹, Mark L Patchett²

Affiliations

¹ Institute of Fundamental Sciences, College of Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. Electronic address: g.norris@massey.ac.nz.
² 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.

PMID: 27662231
DOI: 10.1016/j.sbi.2016.09.003

Abstract

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.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

Bacteriocins / antagonists & inhibitors
Bacteriocins / chemistry
Bacteriocins / metabolism*
Glycosylation

Substances

Bacteriocins