1CIX

THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB

1CIX の概要

• エントリーDOI: 10.2210/pdb1cix/pdb
• NMR情報: BMRB: 5268
• 分子名称: PROTEIN (TACHYSTATIN A) (1 entity in total)
• 機能のキーワード: antimicrobial peptide, chitin-binding peptide
• 由来する生物種: Tachypleus tridentatus
• 細胞内の位置: Secreted: Q9U8X3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5067.86

構造登録者

Fujitani, N.,Kawabata, S.,Osaki, T.,Kumaki, Y.,Demura, M.,Nitta, K.,Kawano, K. (登録日: 1999-04-06, 公開日: 2002-05-01, 最終更新日: 2024-10-30)

主引用文献

Fujitani, N.,Kawabata, S.,Osaki, T.,Kumaki, Y.,Demura, M.,Nitta, K.,Kawano, K.
Structure of the antimicrobial peptide tachystatin A.
J.Biol.Chem., 277:23651-23657, 2002

PubMed 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 beta-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 omega-agatoxin IVA isolated from spider toxin and mammalian defensins, and we predicted that omega-agatoxin IVA also have the antifungal activity. These structural comparisons and functional correspondences suggest that tachystatin A and omega-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 omega-agatoxin IVA also showed chitin-binding activities in this study. Tachystatin A and omega-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 Phe(9) of tachystatin A might be an essential residue for binding to chitin.

PubMed: 11959852
DOI: 10.1074/jbc.M111120200

実験手法

SOLUTION NMR