2K9B

Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy

2K9B の概要

• エントリーDOI: 10.2210/pdb2k9b/pdb
• 分子名称: Dermadistinctin-K (1 entity in total)
• 機能のキーワード: amphipathic alpha-helix, membrane protein structure determination, c-terminal carboxyamidation, antimicrobial protein, amphibian defense peptide, antibiotic, antimicrobial, secreted
• 細胞内の位置: Secreted: P83638
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3156.70

構造登録者

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. (登録日: 2008-10-07, 公開日: 2009-04-14, 最終更新日: 2024-11-20)

主引用文献

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

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: 19289046
DOI: 10.1016/j.bpj.2008.11.063

実験手法

SOLUTION NMR