7K1M
Peptide from stony coral Heliofungia actiniformis: Hact-1
Summary for 7K1M
| Entry DOI | 10.2210/pdb7k1m/pdb |
| NMR Information | BMRB: 30792 |
| Descriptor | GLY-CYS-HIS-TYR-THR-PRO-PHE-GLY-LEU-ILE-CYS-PHE peptide (1 entity in total) |
| Functional Keywords | beta-hairpin, unknown function |
| Biological source | Heliofungia actiniformis |
| Total number of polymer chains | 1 |
| Total formula weight | 1358.61 |
| Authors | Daly, N.L.,Schmidt, C.A. (deposition date: 2020-09-08, release date: 2020-11-25, Last modification date: 2024-10-16) |
| Primary citation | Schmidt, C.A.,Wilson, D.T.,Cooke, I.,Potriquet, J.,Tungatt, K.,Muruganandah, V.,Boote, C.,Kuek, F.,Miles, J.J.,Kupz, A.,Ryan, S.,Loukas, A.,Bansal, P.S.,Takjoo, R.,Miller, D.J.,Peigneur, S.,Tytgat, J.,Daly, N.L. Identification and Characterization of a Peptide from the Stony Coral Heliofungia actiniformis . J.Nat.Prod., 83:3454-3463, 2020 Cited by PubMed Abstract: Marine organisms produce a diverse range of toxins and bioactive peptides to support predation, competition, and defense. The peptide repertoires of stony corals (order Scleractinia) remain relatively understudied despite the presence of tentacles used for predation and defense that are likely to contain a range of bioactive compounds. Here, we show that a tentacle extract from the mushroom coral, , contains numerous peptides with a range of molecular weights analogous to venom profiles from species such as cone snails. Using NMR spectroscopy and mass spectrometry we characterized a 12-residue peptide (Hact-1) with a new sequence (GCHYTPFGLICF) and well-defined β-hairpin structure stabilized by a single disulfide bond. The sequence is encoded within the genome of the coral and expressed in the polyp body tissue. The structure present is common among toxins and venom peptides, but Hact-1 does not show activity against select examples of Gram-positive and Gram-negative bacteria or a range of ion channels, common properties of such peptides. Instead, it appears to have a limited effect on human peripheral blood mononuclear cells, but the ecological function of the peptide remains unknown. The discovery of this peptide from is likely to be the first of many from this and related species. PubMed: 33166137DOI: 10.1021/acs.jnatprod.0c00981 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report






