The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif

Naoki Fujitani, Takahide Kouno, Taku Nakahara, Kenji Takaya, Tsukasa Osaki, Shun-Ichiro Kawabata, Mineyuki Mizuguchi, Tomoyasu Aizawa, Makoto Demura, Shin Ichiro Nishimura, Keiichi Kawano

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Tachystatin B is an antimicrobial and a chitin-binding peptide isolated from the Japanese horseshoe crab (Tachypleus tridentatus) consisting of two isopeptides called tachystatin BI and B2. We have determined their solution structures using NMR experiments and distance geometry calculations. The 20 best converged structures of tachystatin B1 and B2 exhibited root mean square deviations of 0.46 and 0.49 Å, respectively, for the backbone atoms in Cys4-Arg4O. Both structures have identical conformations, and they contain a short antiparallel β-sheet with an inhibitory cystine-knot (ICI) motif that is distributed widely in the antagonists for voltage-gated ion channels, although tachystatin B does not have neurotoxic activity. The structural homology search provided several peptides with structures similar to that of tachystatin B. However, most of them have the advanced functions such as insecticidal activity, suggesting that tachystatin B may be a kind of ancestor of antimicrobial peptide in the molecular evolutionary history. Tachystatin B also displays a significant structural similarity to tachystatin A, which is member of the tachystatin family. The structural comparison of both tachystatins indicated that Tyr14 and Arg17 in the long loop between the first and second strands might be the essential residues for binding to chitin.

Original languageEnglish
Pages (from-to)269-279
Number of pages11
JournalJournal of Peptide Science
Volume13
Issue number4
DOIs
Publication statusPublished - Apr 1 2007

Fingerprint

Cystine Knot Motifs
Horseshoe Crabs
Cystine
Chitin
Peptides
Ion Channels
Conformations
History
Nuclear magnetic resonance
Atoms
Geometry
Electric potential
peptide B
Experiments

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

Cite this

The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif. / Fujitani, Naoki; Kouno, Takahide; Nakahara, Taku; Takaya, Kenji; Osaki, Tsukasa; Kawabata, Shun-Ichiro; Mizuguchi, Mineyuki; Aizawa, Tomoyasu; Demura, Makoto; Nishimura, Shin Ichiro; Kawano, Keiichi.

In: Journal of Peptide Science, Vol. 13, No. 4, 01.04.2007, p. 269-279.

Research output: Contribution to journalArticle

Fujitani, N, Kouno, T, Nakahara, T, Takaya, K, Osaki, T, Kawabata, S-I, Mizuguchi, M, Aizawa, T, Demura, M, Nishimura, SI & Kawano, K 2007, 'The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif', Journal of Peptide Science, vol. 13, no. 4, pp. 269-279. https://doi.org/10.1002/psc.846
Fujitani, Naoki ; Kouno, Takahide ; Nakahara, Taku ; Takaya, Kenji ; Osaki, Tsukasa ; Kawabata, Shun-Ichiro ; Mizuguchi, Mineyuki ; Aizawa, Tomoyasu ; Demura, Makoto ; Nishimura, Shin Ichiro ; Kawano, Keiichi. / The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif. In: Journal of Peptide Science. 2007 ; Vol. 13, No. 4. pp. 269-279.
@article{d78c9e76f3534fd793c64b5856e610dd,
title = "The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif",
abstract = "Tachystatin B is an antimicrobial and a chitin-binding peptide isolated from the Japanese horseshoe crab (Tachypleus tridentatus) consisting of two isopeptides called tachystatin BI and B2. We have determined their solution structures using NMR experiments and distance geometry calculations. The 20 best converged structures of tachystatin B1 and B2 exhibited root mean square deviations of 0.46 and 0.49 {\AA}, respectively, for the backbone atoms in Cys4-Arg4O. Both structures have identical conformations, and they contain a short antiparallel β-sheet with an inhibitory cystine-knot (ICI) motif that is distributed widely in the antagonists for voltage-gated ion channels, although tachystatin B does not have neurotoxic activity. The structural homology search provided several peptides with structures similar to that of tachystatin B. However, most of them have the advanced functions such as insecticidal activity, suggesting that tachystatin B may be a kind of ancestor of antimicrobial peptide in the molecular evolutionary history. Tachystatin B also displays a significant structural similarity to tachystatin A, which is member of the tachystatin family. The structural comparison of both tachystatins indicated that Tyr14 and Arg17 in the long loop between the first and second strands might be the essential residues for binding to chitin.",
author = "Naoki Fujitani and Takahide Kouno and Taku Nakahara and Kenji Takaya and Tsukasa Osaki and Shun-Ichiro Kawabata and Mineyuki Mizuguchi and Tomoyasu Aizawa and Makoto Demura and Nishimura, {Shin Ichiro} and Keiichi Kawano",
year = "2007",
month = "4",
day = "1",
doi = "10.1002/psc.846",
language = "English",
volume = "13",
pages = "269--279",
journal = "Journal of Peptide Science",
issn = "1075-2617",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

T1 - The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif

AU - Fujitani, Naoki

AU - Kouno, Takahide

AU - Nakahara, Taku

AU - Takaya, Kenji

AU - Osaki, Tsukasa

AU - Kawabata, Shun-Ichiro

AU - Mizuguchi, Mineyuki

AU - Aizawa, Tomoyasu

AU - Demura, Makoto

AU - Nishimura, Shin Ichiro

AU - Kawano, Keiichi

PY - 2007/4/1

Y1 - 2007/4/1

N2 - Tachystatin B is an antimicrobial and a chitin-binding peptide isolated from the Japanese horseshoe crab (Tachypleus tridentatus) consisting of two isopeptides called tachystatin BI and B2. We have determined their solution structures using NMR experiments and distance geometry calculations. The 20 best converged structures of tachystatin B1 and B2 exhibited root mean square deviations of 0.46 and 0.49 Å, respectively, for the backbone atoms in Cys4-Arg4O. Both structures have identical conformations, and they contain a short antiparallel β-sheet with an inhibitory cystine-knot (ICI) motif that is distributed widely in the antagonists for voltage-gated ion channels, although tachystatin B does not have neurotoxic activity. The structural homology search provided several peptides with structures similar to that of tachystatin B. However, most of them have the advanced functions such as insecticidal activity, suggesting that tachystatin B may be a kind of ancestor of antimicrobial peptide in the molecular evolutionary history. Tachystatin B also displays a significant structural similarity to tachystatin A, which is member of the tachystatin family. The structural comparison of both tachystatins indicated that Tyr14 and Arg17 in the long loop between the first and second strands might be the essential residues for binding to chitin.

AB - Tachystatin B is an antimicrobial and a chitin-binding peptide isolated from the Japanese horseshoe crab (Tachypleus tridentatus) consisting of two isopeptides called tachystatin BI and B2. We have determined their solution structures using NMR experiments and distance geometry calculations. The 20 best converged structures of tachystatin B1 and B2 exhibited root mean square deviations of 0.46 and 0.49 Å, respectively, for the backbone atoms in Cys4-Arg4O. Both structures have identical conformations, and they contain a short antiparallel β-sheet with an inhibitory cystine-knot (ICI) motif that is distributed widely in the antagonists for voltage-gated ion channels, although tachystatin B does not have neurotoxic activity. The structural homology search provided several peptides with structures similar to that of tachystatin B. However, most of them have the advanced functions such as insecticidal activity, suggesting that tachystatin B may be a kind of ancestor of antimicrobial peptide in the molecular evolutionary history. Tachystatin B also displays a significant structural similarity to tachystatin A, which is member of the tachystatin family. The structural comparison of both tachystatins indicated that Tyr14 and Arg17 in the long loop between the first and second strands might be the essential residues for binding to chitin.

UR - http://www.scopus.com/inward/record.url?scp=34247351569&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34247351569&partnerID=8YFLogxK

U2 - 10.1002/psc.846

DO - 10.1002/psc.846

M3 - Article

C2 - 17394123

AN - SCOPUS:34247351569

VL - 13

SP - 269

EP - 279

JO - Journal of Peptide Science

JF - Journal of Peptide Science

SN - 1075-2617

IS - 4

ER -