Solution Structure of LCI, a Novel Antimicrobial Peptide from Bacillus subtilis
- 影响因子：
0.0
- DOI码：
10.1021/bi200123w
- 发表刊物：
Biochemistry
- 摘要：
LCI, a 47-residue cationic antimicrobial peptide (AMP) found in Bacillus subtilis, is one of the main effective components that have strong antimicrobial activity against Xanthomonas campestris pv Oryzea and Pseudomonas solanacearum PE1, etc. To provide insight into the activity of the peptide, we used nuclear magnetic resonance spectroscopy to determine the structure of recombinant LCI. The solution structure of LCI has a novel topology, containing a four-strand antiparallel β-sheet as the dominant secondary structure. It is the first structure of the LCI protein family. Different from any known β-structure AMPs, LCI contains no disulfide bridge or circular structure, suggesting that LCI is also a novel β-structure AMP.
- 论文编号：
29
- 卷号：
50
- 页面范围：
3621-7
- 是否译文：
否
- 发表时间：
2011-01-01
- 发布期刊链接：
- 第一作者：
Gong W
- 通讯作者：
Lu G,Xia Bin
- 全部作者：
Chen Z,Wang J
