抄録
The solution structure of antimicrobial peptide tachystatin A from the Japanese horseshoe crab (Tachypleus tridentatus) was determined by two-dimensional nuclear magnetic resonance measurements and distance-restrained simulated annealing calculations. The correct pairs of disulfide bonds were also confirmed in this study. The obtained structure has a cysteine-stabilized triple-stranded β-sheet as a dominant secondary structure and shows an amphiphilic folding observed in many membrane-interactive peptides. Interestingly, tachystatin A shares structural similarities with the calcium channel antagonist ω-agatoxin IVA isolated from spider toxin and mammalian defensins, and we predicted that ω-agatoxin IVA also have the antifungal activity. These structural comparisons and functional correspondences suggest that tachystatin A and ω-agatoxin IVA may exert the antimicrobial activity in a manner similar to defensins, and we have confirmed such activity using fungal culture assays. Furthermore, tachystatin A is a chitin-binding peptide, and ω-agatoxin IVA also showed chitin-binding activities in this study. Tachystatin A and ω-agatoxin IVA showed no structural homology with well known chitin-binding motifs, suggesting that their structures belong to a novel family of chitin-binding peptides. Comparison of their structures with those of cellulose-binding proteins indicated that Phe9 of tachystatin A might be an essential residue for binding to chitin.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 23651-23657 |
| ページ数 | 7 |
| ジャーナル | Journal of Biological Chemistry |
| 巻 | 277 |
| 発行部数 | 26 |
| DOI | |
| 出版物ステータス | 出版済み - 6 28 2002 |
| 外部発表 | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
これを引用
Structure of the antimicrobial peptide tachystatin A. / Fujitani, Naoki; Kawabata, Shun-Ichiro; Osaki, Tsukasa; Kumaki, Yasuhiro; Demura, Makoto; Nitta, Katsutoshi; Kawano, Keiichi.
：: Journal of Biological Chemistry, 巻 277, 番号 26, 28.06.2002, p. 23651-23657.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Structure of the antimicrobial peptide tachystatin A
AU - Fujitani, Naoki
AU - Kawabata, Shun-Ichiro
AU - Osaki, Tsukasa
AU - Kumaki, Yasuhiro
AU - Demura, Makoto
AU - Nitta, Katsutoshi
AU - Kawano, Keiichi
PY - 2002/6/28
Y1 - 2002/6/28
N2 - The solution structure of antimicrobial peptide tachystatin A from the Japanese horseshoe crab (Tachypleus tridentatus) was determined by two-dimensional nuclear magnetic resonance measurements and distance-restrained simulated annealing calculations. The correct pairs of disulfide bonds were also confirmed in this study. The obtained structure has a cysteine-stabilized triple-stranded β-sheet as a dominant secondary structure and shows an amphiphilic folding observed in many membrane-interactive peptides. Interestingly, tachystatin A shares structural similarities with the calcium channel antagonist ω-agatoxin IVA isolated from spider toxin and mammalian defensins, and we predicted that ω-agatoxin IVA also have the antifungal activity. These structural comparisons and functional correspondences suggest that tachystatin A and ω-agatoxin IVA may exert the antimicrobial activity in a manner similar to defensins, and we have confirmed such activity using fungal culture assays. Furthermore, tachystatin A is a chitin-binding peptide, and ω-agatoxin IVA also showed chitin-binding activities in this study. Tachystatin A and ω-agatoxin IVA showed no structural homology with well known chitin-binding motifs, suggesting that their structures belong to a novel family of chitin-binding peptides. Comparison of their structures with those of cellulose-binding proteins indicated that Phe9 of tachystatin A might be an essential residue for binding to chitin.
AB - The solution structure of antimicrobial peptide tachystatin A from the Japanese horseshoe crab (Tachypleus tridentatus) was determined by two-dimensional nuclear magnetic resonance measurements and distance-restrained simulated annealing calculations. The correct pairs of disulfide bonds were also confirmed in this study. The obtained structure has a cysteine-stabilized triple-stranded β-sheet as a dominant secondary structure and shows an amphiphilic folding observed in many membrane-interactive peptides. Interestingly, tachystatin A shares structural similarities with the calcium channel antagonist ω-agatoxin IVA isolated from spider toxin and mammalian defensins, and we predicted that ω-agatoxin IVA also have the antifungal activity. These structural comparisons and functional correspondences suggest that tachystatin A and ω-agatoxin IVA may exert the antimicrobial activity in a manner similar to defensins, and we have confirmed such activity using fungal culture assays. Furthermore, tachystatin A is a chitin-binding peptide, and ω-agatoxin IVA also showed chitin-binding activities in this study. Tachystatin A and ω-agatoxin IVA showed no structural homology with well known chitin-binding motifs, suggesting that their structures belong to a novel family of chitin-binding peptides. Comparison of their structures with those of cellulose-binding proteins indicated that Phe9 of tachystatin A might be an essential residue for binding to chitin.
UR - http://www.scopus.com/inward/record.url?scp=0037189558&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037189558&partnerID=8YFLogxK
U2 - 10.1074/jbc.M111120200
DO - 10.1074/jbc.M111120200
M3 - Article
C2 - 11959852
AN - SCOPUS:0037189558
VL - 277
SP - 23651
EP - 23657
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 26
ER -