Journal
ACS CHEMICAL BIOLOGY
Volume 9, Issue 3, Pages 796-801Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb4008106
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Funding
- U.S. National Institutes of Health [GM 58822, S10RR027109-01]
- NIGMS-NIH Chemistry-Biology Interface Training Grant [5T32-GM070421]
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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 a-helices and a well-defined interhelical loop. The two helices span residues 6-16 and 26-35, and the loop region encompasses residues 17-25. The 9-amino-acid loop region contains a beta-S-linked glucose moiety attached to Cys22. Hydrophobic interactions as well as hydrogen bonding are responsible for the well-structured loop region. The three-dimensional structure provides an explanation for the previously reported extraordinary high stability of sublancin 168.
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