1ee7: Difference between revisions
New page: left|200px<br /><applet load="1ee7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ee7" /> '''NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN... |
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[[Image:1ee7.jpg|left|200px]]<br /><applet load="1ee7" size=" | [[Image:1ee7.jpg|left|200px]]<br /><applet load="1ee7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES'''<br /> | '''NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES'''<br /> | ||
==Overview== | ==Overview== | ||
Chrysospermin C is a 19-residue peptaibol capable of forming transmembrane | 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== | ==About this Structure== | ||
1EE7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Apiocrea_chrysosperma Apiocrea chrysosperma] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1EE7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Apiocrea_chrysosperma Apiocrea chrysosperma] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EE7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Anders, R.]] | [[Category: Anders, R.]] | ||
[[Category: Brown, L | [[Category: Brown, L R.]] | ||
[[Category: Heise, B.]] | [[Category: Heise, B.]] | ||
[[Category: Ohlenschlager, O.]] | [[Category: Ohlenschlager, O.]] | ||
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[[Category: peptide antibiotic]] | [[Category: peptide antibiotic]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:48 2008'' | ||
Revision as of 13:26, 21 February 2008
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NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES
OverviewOverview
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 StructureAbout this Structure
1EE7 is a Protein complex structure of sequences from Apiocrea chrysosperma with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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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