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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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Biochem J
410:113-122
(2008)
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PubMed id:
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Structure and mode of action of the antimicrobial peptide arenicin.
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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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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.Park,
J.Cho,
J.Lee,
and
D.G.Lee
(2011).
Membranolytic antifungal activity of arenicin-1 requires the N-terminal tryptophan and the beta-turn arginine.
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Biotechnol Lett,
33,
185-189.
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R.Macháň,
M.Hof,
T.Chernovets,
M.N.Zhmak,
T.V.Ovchinnikova,
and
J.Sýkora
(2011).
Formation of arenicin-1 microdomains in bilayers and their specific lipid interaction revealed by Z-scan FCS.
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Anal Bioanal Chem,
399,
3547-3554.
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C.C.Hughes,
and
W.Fenical
(2010).
Antibacterials from the sea.
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Chemistry,
16,
12512-12525.
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M.U.Hammer,
A.Brauser,
C.Olak,
G.Brezesinski,
T.Goldmann,
T.Gutsmann,
and
J.Andrä
(2010).
Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis.
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Biochem J,
427,
477-488.
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O.G.Travkova,
J.Andrä,
H.Möhwald,
and
G.Brezesinski
(2010).
Conformational properties of arenicins: from the bulk to the air-water interface.
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Chemphyschem,
11,
3262-3268.
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J.Andrä,
M.U.Hammer,
J.Grötzinger,
I.Jakovkin,
B.Lindner,
E.Vollmer,
H.Fedders,
M.Leippe,
and
T.Gutsmann
(2009).
Significance of the cyclic structure and of arginine residues for the antibacterial activity of arenicin-1 and its interaction with phospholipid and lipopolysaccharide model membranes.
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Biol Chem,
390,
337-349.
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R.W.Davis,
D.C.Arango,
H.D.Jones,
M.H.Van Benthem,
D.M.Haaland,
S.M.Brozik,
and
M.B.Sinclair
(2009).
Antimicrobial peptide interactions with silica bead supported bilayers and E. coli: buforin II, magainin II, and arenicin.
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J Pept Sci,
15,
511-522.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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