2K9B
Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy
Summary for 2K9B
| Entry DOI | 10.2210/pdb2k9b/pdb |
| Descriptor | Dermadistinctin-K (1 entity in total) |
| Functional Keywords | amphipathic alpha-helix, membrane protein structure determination, c-terminal carboxyamidation, antimicrobial protein, amphibian defense peptide, antibiotic, antimicrobial, secreted |
| Cellular location | Secreted: P83638 |
| Total number of polymer chains | 1 |
| Total formula weight | 3156.70 |
| Authors | Moraes, C.M.,Verly, R.M.,Resende, J.M.,Aisenbrey, C.,Bemquerer, M.P.,Pilo-Veloso, D.,Valente, A.,Almeida, F.C.L.,Bechinger, B. (deposition date: 2008-10-07, release date: 2009-04-14, Last modification date: 2024-11-20) |
| Primary citation | Verly, R.M.,de Moraes, C.M.,Resende, J.M.,Aisenbrey, C.,Bemquerer, M.P.,Pilo-Veloso, D.,Valente, A.P.,Almeida, F.C.L.,Bechinger, B. Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy. Biophys.J., 96:2194-2203, 2009 Cited by PubMed Abstract: DD K, a peptide first isolated from the skin secretion of the Phyllomedusa distincta frog, has been prepared by solid-phase chemical peptide synthesis and its conformation was studied in trifluoroethanol/water as well as in the presence of sodium dodecyl sulfate and dodecylphosphocholine micelles or small unilamellar vesicles. Multidimensional solution NMR spectroscopy indicates an alpha-helical conformation in membrane environments starting at residue 7 and extending to the C-terminal carboxyamide. Furthermore, DD K has been labeled with (15)N at a single alanine position that is located within the helical core region of the sequence. When reconstituted into oriented phosphatidylcholine membranes the resulting (15)N solid-state NMR spectrum shows a well-defined helix alignment parallel to the membrane surface in excellent agreement with the amphipathic character of DD K. Proton-decoupled (31)P solid-state NMR spectroscopy indicates that the peptide creates a high level of disorder at the level of the phospholipid headgroup suggesting that DD K partitions into the bilayer where it severely disrupts membrane packing. PubMed: 19289046DOI: 10.1016/j.bpj.2008.11.063 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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