2jos: Difference between revisions

Revision as of 17:10, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2jos.png

Template:STRUCTURE 2jos

Solution structure of piscidin in presence of DPC micellesSolution structure of piscidin in presence of DPC micelles

Template:ABSTRACT PUBMED 17253775

About this StructureAbout this Structure

2JOS is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Structure and mechanism of action of the antimicrobial peptide piscidin., Campagna S, Saint N, Molle G, Aumelas A, Biochemistry. 2007 Feb 20;46(7):1771-8. Epub 2007 Jan 25. PMID:17253775

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OCA

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-'''Solution structure of piscidin in presence of DPC micelles'''
+===Solution structure of piscidin in presence of DPC micelles===
-==Overview==
+<!--
-Piscidin, an antibacterial peptide isolated from the mast cells of striped bass, has potent antimicrobial activity against a broad spectrum of pathogens in vitro. We investigated the mechanism of action of this 22-residue cationic peptide by carrying out structural studies and electrophysiological experiments in lipid bilayers. Circular dichroism experiments showed that piscidin was unstructured in water but had a high alpha-helix content in dodecylphosphocholine (DPC) micelles. 1H NMR data in water and TFE confirmed these results and demonstrated that the segment of residues 8-17 adopted an alpha-helical structure in a micellar environment. This molecule has a marked amphipathic character, due to well-defined hydrophobic and hydrophilic sectors. This structure is similar to those determined for other cationic peptides involved in permeabilization of the bacterial membrane. Multichannel experiments with piscidin incorporated into azolectin planar bilayers gave reproducible I-V curves at various peptide concentrations and unambiguously showed that this peptide permeabilized the membrane. This pore forming activity was confirmed by single-channel experiments, with well-defined ion channels obtained at different voltages. The characteristics of the ion channels (voltage dependence, only one or two states of conductance) clearly suggest that piscidin is more likely to permeabilize the membrane by toroidal pore formation rather than via the "barrel-stave" mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_17253775}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17253775 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17253775}}
 ==About this Structure==
-JOS is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOS OCA].
+JOS is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOS OCA].
 ==Reference==
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 [[Category: Micellar environment]]
 [[Category: Piscidin]]
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