1CIX
THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB
Summary for 1CIX
| Entry DOI | 10.2210/pdb1cix/pdb |
| NMR Information | BMRB: 5268 |
| Descriptor | PROTEIN (TACHYSTATIN A) (1 entity in total) |
| Functional Keywords | antimicrobial peptide, chitin-binding peptide |
| Biological source | Tachypleus tridentatus |
| Cellular location | Secreted: Q9U8X3 |
| Total number of polymer chains | 1 |
| Total formula weight | 5067.86 |
| Authors | Fujitani, N.,Kawabata, S.,Osaki, T.,Kumaki, Y.,Demura, M.,Nitta, K.,Kawano, K. (deposition date: 1999-04-06, release date: 2002-05-01, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 11959852DOI: 10.1074/jbc.M111120200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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