Solution Structure of LCI, a Novel Antimicrobial Peptide from Bacillus subtilis
| Autor: | Guang-Ying Lu, Bin Xia, Jinfeng Wang, Zhang-Liang Chen, Weibin Gong |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Magnetic Resonance Spectroscopy
Protein family Protein Conformation Stereochemistry Peptide Bacillus subtilis Xanthomonas campestris Biochemistry Protein Structure Secondary Protein structure Bacterial Proteins Pseudomonas Protein secondary structure chemistry.chemical_classification biology Antimicrobial biology.organism_classification Adenosine Monophosphate Recombinant Proteins Protein Structure Tertiary chemistry Peptides Genome Bacterial Antimicrobial Cationic Peptides |
| Zdroj: | Biochemistry. 50:3621-3627 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi200123w |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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