Abstract:
:Bacteriocins are bacterial peptides with specific activity against competing species. They hold great potential as natural preservatives and for their probiotic effects. We show here nuclear magnetic resonance-based evidence that glycocin F, a 43-amino acid bacteriocin from Lactobacillus plantarum, contains two β-linked N-acetylglucosamine moieties, attached via side chain linkages to a serine via oxygen, and to a cysteine via sulfur. The latter linkage is novel and has helped to establish a new type of post-translational modification, the S-linked sugar. The peptide conformation consists primarily of two α-helices held together by a pair of nested disulfide bonds. The serine-linked sugar is positioned on a short loop sequentially connecting the two helices, while the cysteine-linked sugar presents at the end of a long disordered C-terminal tail. The differing chemical and conformational stabilities of the two N-actetylglucosamine moieties provide clues about the possible mode of action of this bacteriostatic peptide.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Venugopal H,Edwards PJ,Schwalbe M,Claridge JK,Libich DS,Stepper J,Loo T,Patchett ML,Norris GE,Pascal SMdoi
10.1021/bi200217usubject
Has Abstractpub_date
2011-04-12 00:00:00pages
2748-55issue
14eissn
0006-2960issn
1520-4995journal_volume
50pub_type
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