1ee7: Difference between revisions

Revision as of 00:33, 1 July 2008

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Template:STRUCTURE 1ee7

NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLESNMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES

Template:ABSTRACT PUBMED 10712611

About this StructureAbout this Structure

Full experimental 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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 {{STRUCTURE_1ee7|  PDB=1ee7  |  SCENE=  }}
-'''NMR STRUCTURE OF THE PEPTAIBOL CHRYSOSPERMIN C BOUND TO DPC MICELLES'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10712611}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10712611 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10712611}}
 ==About this Structure==
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EE7 OCA].
+Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EE7 OCA].
 ==Reference==
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 [[Category: Peptaibol]]
 [[Category: Peptide antibiotic]]
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