NMR structure of the S-linked glycopeptide sublancin 168.

NMR structure of the S-linked glycopeptide sublancin 168.
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S连锁糖肽Sublancin的NMR结构168。

DOI:
10.1021/cb4008106
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发表时间:
2014-03-21
影响因子:
4
通讯作者:
van der Donk, Wilfred A.
van der Donk, Wilfred A.
中科院分区:
生物学2区
文献类型:
--
作者:
De Gonzalo, Chantal V. Garcia;Zhu, Lingyang;Oman, Trent J.;van der Donk, Wilfred A.

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Sublancin 168是一小组糖基化抗菌肽(称为糖蛋白)的成员。枯草芽孢杆菌168产生的37个氨基酸的肽sublancin 168的溶液结构已通过核磁共振(NMR)光谱得到解决。Sublancin由两个α-螺旋和一个明确的螺旋间环组成。两个螺旋跨越残基6-16和26-35,环区涵盖残基17-25。9-氨基酸环区含有与Cys 22连接的β-S-连接的葡萄糖部分。疏水相互作用以及氢键是负责良好结构的环区域。三维结构为先前报道的sublancin 168非常高的稳定性提供了解释。
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.
DOI: 10.1126/science.1198461
发表时间: 2011-02-04
期刊: Science (New York, N.Y.)
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