期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 40, 期 -, 页码 112-119出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2016.09.003
关键词
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资金
- Royal Society of New Zealand Marsden Fund [MAU0504]
- Maurice Wilkins Centre for Molecular Biodiscovery School of Biological Sciences
- University of Auckland, New Zealand
- Massey University
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 alpha/alpha folds, are deposited in the PDB. Each structure contains a monosaccharide beta-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.
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