1EE7

NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES

Summary for 1EE7

• Entry DOI: 10.2210/pdb1ee7/pdb
• Related: 1AMT 1DLZ 1GQ0 1IH9 1JOH 1M24 1OB4 1OB6 1OB7 1R9U
• NMR Information: BMRB: 4604
• Related PRD ID: PRD_000162
• Descriptor: CHRYSOSPERMIN C (1 entity in total)
• Functional Keywords: chrysospermin c, peptaibol, antibacterial, antifungal, antibiotic
• Biological source: HYPOMYCES CHRYSOSPERMUS
• Total number of polymer chains: 1
• Total formula weight: 1896.24

Authors

Anders, R.,Ohlenschlager, O.,Soskic, V.,Wenschuh, H.,Heise, B.,Brown, L.R. (deposition date: 2000-01-31, release date: 2000-05-10, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

SOLUTION NMR