Structure of the antimicrobial peptide tachystatin A

Naoki Fujitani, Shun-Ichiro Kawabata, Tsukasa Osaki, Yasuhiro Kumaki, Makoto Demura, Katsutoshi Nitta, Keiichi Kawano

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)23651-23657
Number of pages7
JournalJournal of Biological Chemistry
Volume277
Issue number26
DOIs
Publication statusPublished - Jun 28 2002
Externally publishedYes

Fingerprint

Agatoxins
Chitin
Peptides
Defensins
Horseshoe Crabs
Pair Bond
Magnetic resonance measurement
Spiders
Calcium Channel Blockers
Simulated annealing
Cellulose
Disulfides
Cysteine
tachystatin A
Assays
Carrier Proteins
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Membranes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Fujitani, N., Kawabata, S-I., Osaki, T., Kumaki, Y., Demura, M., Nitta, K., & Kawano, K. (2002). Structure of the antimicrobial peptide tachystatin A. Journal of Biological Chemistry, 277(26), 23651-23657. https://doi.org/10.1074/jbc.M111120200

Structure of the antimicrobial peptide tachystatin A. / Fujitani, Naoki; Kawabata, Shun-Ichiro; Osaki, Tsukasa; Kumaki, Yasuhiro; Demura, Makoto; Nitta, Katsutoshi; Kawano, Keiichi.

In: Journal of Biological Chemistry, Vol. 277, No. 26, 28.06.2002, p. 23651-23657.

Research output: Contribution to journalArticle

Fujitani, N, Kawabata, S-I, Osaki, T, Kumaki, Y, Demura, M, Nitta, K & Kawano, K 2002, 'Structure of the antimicrobial peptide tachystatin A', Journal of Biological Chemistry, vol. 277, no. 26, pp. 23651-23657. https://doi.org/10.1074/jbc.M111120200
Fujitani N, Kawabata S-I, Osaki T, Kumaki Y, Demura M, Nitta K et al. Structure of the antimicrobial peptide tachystatin A. Journal of Biological Chemistry. 2002 Jun 28;277(26):23651-23657. https://doi.org/10.1074/jbc.M111120200
Fujitani, Naoki ; Kawabata, Shun-Ichiro ; Osaki, Tsukasa ; Kumaki, Yasuhiro ; Demura, Makoto ; Nitta, Katsutoshi ; Kawano, Keiichi. / Structure of the antimicrobial peptide tachystatin A. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 26. pp. 23651-23657.
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