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PDBsum entry 2jsb
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Antimicrobial protein
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PDB id
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2jsb
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References listed in PDB file
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Key reference
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Title
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Structure and mode of action of the antimicrobial peptide arenicin.
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Authors
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J.Andrä,
I.Jakovkin,
J.Grötzinger,
O.Hecht,
A.D.Krasnosdembskaya,
T.Goldmann,
T.Gutsmann,
M.Leippe.
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Ref.
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Biochem J, 2008,
410,
113-122.
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PubMed id
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Abstract
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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.
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