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PDBsum entry 2mn5
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Antimicrobial protein
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PDB id
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2mn5
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References listed in PDB file
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Key reference
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Title
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Copsin, A novel peptide-Based fungal antibiotic interfering with the peptidoglycan synthesis.
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Authors
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A.Essig,
D.Hofmann,
D.Münch,
S.Gayathri,
M.Künzler,
P.T.Kallio,
H.G.Sahl,
G.Wider,
T.Schneider,
M.Aebi.
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Ref.
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J Biol Chem, 2014,
289,
34953-34964.
[DOI no: ]
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PubMed id
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Abstract
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Fungi and bacteria compete with an arsenal of secreted molecules for their
ecological niche. This repertoire represents a rich and inexhaustible source for
antibiotics and fungicides. Antimicrobial peptides are an emerging class of
fungal defense molecules that are promising candidates for pharmaceutical
applications. Based on a co-cultivation system, we studied the interaction of
the coprophilous basidiomycete Coprinopsis cinerea with different bacterial
species and identified a novel defensin, copsin. The polypeptide was
recombinantly produced in Pichia pastoris, and the three-dimensional structure
was solved by NMR. The cysteine stabilized α/β-fold with a unique disulfide
connectivity, and an N-terminal pyroglutamate rendered copsin extremely stable
against high temperatures and protease digestion. Copsin was bactericidal
against a diversity of Gram-positive bacteria, including human pathogens such as
Enterococcus faecium and Listeria monocytogenes. Characterization of the
antibacterial activity revealed that copsin bound specifically to the
peptidoglycan precursor lipid II and therefore interfered with the cell wall
biosynthesis. In particular, and unlike lantibiotics and other defensins, the
third position of the lipid II pentapeptide is essential for effective copsin
binding. The unique structural properties of copsin make it a possible scaffold
for new antibiotics.
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