1ee7
From Proteopedia
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| - | [[Image:1ee7.jpg|left|200px]] | + | [[Image:1ee7.jpg|left|200px]] |
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| - | '''NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES''' | + | {{Structure |
| + | |PDB= 1ee7 |SIZE=350|CAPTION= <scene name='initialview01'>1ee7</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EE7 is a [ | + | 1EE7 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Apiocrea_chrysosperma Apiocrea chrysosperma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EE7 OCA]. |
==Reference== | ==Reference== | ||
| - | The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles., Anders R, Ohlenschlager O, Soskic V, Wenschuh H, Heise B, Brown LR, Eur J Biochem. 2000 Mar;267(6):1784-94. PMID:[http:// | + | The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles., Anders R, Ohlenschlager O, Soskic V, Wenschuh H, Heise B, Brown LR, Eur J Biochem. 2000 Mar;267(6):1784-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10712611 10712611] |
[[Category: Apiocrea chrysosperma]] | [[Category: Apiocrea chrysosperma]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:54:27 2008'' |
Revision as of 08:54, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES
Overview
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.
About this Structure
1EE7 is a Protein complex structure of sequences from Apiocrea chrysosperma. Full crystallographic information is available from OCA.
Reference
The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles., Anders R, Ohlenschlager O, Soskic V, Wenschuh H, Heise B, Brown LR, Eur J Biochem. 2000 Mar;267(6):1784-94. PMID:10712611
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