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NMR structure of the S-linked glycopeptide sublancin 168.

Abstract：

: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 loop region encompasses residues 17-25. The 9-amino-acid loop region contains a β-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.

journal_name

ACS Chem Biol

journal_title

ACS chemical biology

authors

Garcia De Gonzalo CV,Zhu L,Oman TJ,van der Donk WA

doi

10.1021/cb4008106

subject

Has Abstract

pub_date

2014-03-21 00:00:00

pages

796-801

issue

3

eissn

1554-8929

issn

1554-8937

journal_volume

9

pub_type

杂志文章

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