title: Solution structure of LCI, a novel antimicrobial peptide from Bacillus subtilis.
abstract: 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.
authors: The National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing, China 100871.
authors: Weibin
authors: W
authors: Gong
authors: Jinfeng
authors: J
authors: Wang
authors: Zhangliang
authors: Z
authors: Chen
authors: Bin
authors: B
authors: Xia
authors: Guangying
authors: G
authors: Lu
mesh_terms: D000249:Adenosine Monophosphate / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D016680:Genome, Bacterial; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D016959:Xanthomonas campestris / Q000378:metabolism
chemical_list: D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; C559264:LCI peptide, Bacillus subtilis; D010455:Peptides; D011994:Recombinant Proteins; D000249:Adenosine Monophosphate