NMR Structure of the S-Linked Glycopeptide Sublancin 168
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چکیده
منابع مشابه
NMR Structure of the S-Linked Glycopeptide Sublancin 168
Sublancin 168 is a member of a small group of glycosylated antimicrobial peptides known as glycocins. The solution structure of sublancin 168, a 37-amino-acid peptide produced by Bacillus subtilis 168, has been solved by nuclear magnetic resonance (NMR) spectroscopy. Sublancin comprises two α-helices and a well-defined interhelical loop. The two helices span residues 6-16 and 26-35, and the loo...
متن کاملSublancin is not a lantibiotic but an S-linked glycopeptide
Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a cysteine residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro, and the enzyme is shown to have relaxed substrate specificity, allowing the preparation of analogs of sublancin. Glycosylation is essential for its antimicrobial activity.
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SunS is a novel S-glycosyltransferase involved in the biosynthesis of the antimicrobial peptide sublancin. It selectively modifies Cys22 in a 56 amino acid peptide substrate SunA and can accept a variety of NDP sugars. This study reports the substrate selectivity with regard to the peptide substrate and the antimicrobial activity of the resulting sublancin analogues. The results suggest that Su...
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15 صفحه اولThiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168.
Thiol-disulfide oxidoreductases are required for disulfide bond formation in proteins that are exported from the cytoplasm. Four enzymes of this type, termed BdbA, BdbB, BdbC, and BdbD, have been identified in the Gram-positive eubacterium Bacillus subtilis. BdbC and BdbD have been shown to be critical for the folding of a protein required for DNA uptake during natural competence. In contrast, ...
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ژورنال
عنوان ژورنال: ACS Chemical Biology
سال: 2014
ISSN: 1554-8929,1554-8937
DOI: 10.1021/cb4008106