6G4I
The solution NMR structure of brevinin-1BYa in 33% trifluoroethanol
Summary for 6G4I
| Entry DOI | 10.2210/pdb6g4i/pdb |
| NMR Information | BMRB: 34250 |
| Descriptor | Brevinin-1BYa (1 entity in total) |
| Functional Keywords | cationic, rana-box, antimicrobial peptide, antimicrobial protein |
| Biological source | Rana boylii (Foothill yellow-legged frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 2613.32 |
| Authors | Timmons, P.B.,O'Flynn, D.P.,Conlon, J.M.,Hewage, C.M. (deposition date: 2018-03-27, release date: 2019-10-09, Last modification date: 2024-11-20) |
| Primary citation | Timmons, P.B.,O'Flynn, D.,Conlon, J.M.,Hewage, C.M. Structural and positional studies of the antimicrobial peptide brevinin-1BYa in membrane-mimetic environments. J.Pept.Sci., 25:e3208-e3208, 2019 Cited by PubMed Abstract: Brevinin-1BYa (FLPILASLAAKFGPKLFCLVTKKC), first isolated from skin secretions of the foothill yellow-legged frog Rana boylii, shows broad-spectrum activity, being particularly effective against opportunistic yeast pathogens. The structure of brevinin-1BYa was investigated in various solution and membrane-mimicking environments by proton nuclear magnetic resonance ( H-NMR) spectroscopy and molecular modelling. The peptide does not possess a secondary structure in aqueous solution. In a 33% 2,2,2-trifluoroethanol (TFE-d )-H O solvent mixture, as well as in membrane-mimicking sodium dodecyl sulfate and dodecylphosphocholine micelles, the peptide's structure is characterised by a flexible helix-hinge-helix motif, with the hinge located at the Gly /Pro residues, and the two α-helices extending from Pro to Phe and from Pro to Thr . Positional studies involving the peptide in sodium dodecyl sulfate and dodecylphosphocholine micelles using 5-doxyl-labelled stearic acid and manganese chloride paramagnetic probes show that the peptide's helical segments lie parallel to the micellar surface, with the residues on the hydrophobic face of the amphipathic helices facing towards the micelle core and the hydrophilic residues pointing outwards, suggesting that the peptide exerts its biological activity by a non-pore-forming mechanism. PubMed: 31721374DOI: 10.1002/psc.3208 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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