2jsb

From Proteopedia

Revision as of 06:14, 13 February 2008

Solution structure of arenicin-1

Overview

The solution structure and the mode of action of arenicin isoform 1, an, antimicrobial peptide with a unique 18-residue loop structure, from the, lugworm Arenicola marina were elucidated here. Arenicin folds into a, two-stranded antiparallel beta-sheet. It exhibits high antibacterial, activity at 37 and 4 degrees C against Gram-negative bacteria, including, polymyxin B-resistant Proteus mirabilis. Bacterial killing occurs within, minutes and is accompanied by membrane permeabilization, membrane, detachment and release of cytoplasm. Interaction of arenicin with, reconstituted membranes that mimic the lipopolysaccharide-containing outer, membrane or the phospholipid-containing plasma membrane of Gram-negative, bacteria exhibited no pronounced lipid specificity. Arenicin-induced, current fluctuations in planar lipid bilayers correspond to the formation, of short-lived heterogeneously structured lesions. Our results strongly, suggest that membrane interaction plays a pivotal role in the, antibacterial activity of arenicin.

About this Structure

2JSB is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Structure and mode of action of the antimicrobial peptide arenicin., Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M, Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487

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