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7K1M

Peptide from stony coral Heliofungia actiniformis: Hact-1

Summary for 7K1M
Entry DOI10.2210/pdb7k1m/pdb
NMR InformationBMRB: 30792
DescriptorGLY-CYS-HIS-TYR-THR-PRO-PHE-GLY-LEU-ILE-CYS-PHE peptide (1 entity in total)
Functional Keywordsbeta-hairpin, unknown function
Biological sourceHeliofungia actiniformis
Total number of polymer chains1
Total formula weight1358.61
Authors
Daly, N.L.,Schmidt, C.A. (deposition date: 2020-09-08, release date: 2020-11-25, Last modification date: 2024-10-16)
Primary citationSchmidt, 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: 33166137
DOI: 10.1021/acs.jnatprod.0c00981
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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