1EE7

NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES

1EE7 の概要

• エントリーDOI: 10.2210/pdb1ee7/pdb
• 関連するPDBエントリー: 1AMT 1DLZ 1GQ0 1IH9 1JOH 1M24 1OB4 1OB6 1OB7 1R9U
• NMR情報: BMRB: 4604
• 関連するBIRD辞書のPRD_ID: PRD_000162
• 分子名称: CHRYSOSPERMIN C (1 entity in total)
• 機能のキーワード: chrysospermin c, peptaibol, antibacterial, antifungal, antibiotic
• 由来する生物種: HYPOMYCES CHRYSOSPERMUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1896.24

構造登録者

Anders, R.,Ohlenschlager, O.,Soskic, V.,Wenschuh, H.,Heise, B.,Brown, L.R. (登録日: 2000-01-31, 公開日: 2000-05-10, 最終更新日: 2023-11-15)

主引用文献

Anders, R.,Ohlenschlager, O.,Soskic, V.,Wenschuh, H.,Heise, B.,Brown, L.R.
The NMR Solution Structure of the Ion Channel Peptaibol Chrysospermin C Bound to Dodecylphosphocholine Micelles.
Eur.J.Biochem., 267:1784-, 2000

PubMed Abstract: Chrysospermin C is a 19-residue peptaibol capable of forming transmembrane ion channels in phospholipid bilayers. The conformation of chrysospermin C bound to dodecylphosphocholine micelles has been solved using heteronuclear NMR spectroscopy. Selective 15N-labeling and 13C-labeling of specific alpha-aminoisobutyric acid residues was used to obtain complete stereospecific assignments for all eight alpha-aminoisobutyric acid residues. Structures were calculated using 339 distance constraints and 40 angle constraints obtained from NMR data. The NMR structures superimpose with mean global rmsd values to the mean structure of 0. 27 A (backbone heavy atoms) and 0.42 A (all heavy atoms). Chrysospermin C bound to decylphosphocholine micelles displays two well-defined helices at the N-terminus (residues Phe1-Aib9) and C-terminus (Aib13-Trp-ol19). A slight bend preceding Pro14, i.e. encompassing residues 10-12, results in an angle of approximately 38 degrees between the mean axes of the two helical regions. The bend structure observed for chrysospermin C is compatible with the sequences of all 18 long peptaibols and may represent a common 'active' conformation. The structure of chrysospermin C shows clear hydrophobic and hydrophilic surfaces which would be appropriate for the formation of oligomeric ion channels.

PubMed: 10712611
DOI: 10.1046/J.1432-1327.2000.01177.X

実験手法

SOLUTION NMR