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PDBsum entry 3gnu
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References listed in PDB file
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Key reference
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Title
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A common toxin fold mediates microbial attack and plant defense.
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Authors
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C.Ottmann,
B.Luberacki,
I.Küfner,
W.Koch,
F.Brunner,
M.Weyand,
L.Mattinen,
M.Pirhonen,
G.Anderluh,
H.U.Seitz,
T.Nürnberger,
C.Oecking.
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Ref.
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Proc Natl Acad Sci U S A, 2009,
106,
10359-10364.
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PubMed id
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Abstract
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Many plant pathogens secrete toxins that enhance microbial virulence by killing
host cells. Usually, these toxins are produced by particular microbial taxa,
such as bacteria or fungi. In contrast, many bacterial, fungal and oomycete
species produce necrosis and ethylene-inducing peptide 1 (Nep1)-like proteins
(NLPs) that trigger leaf necrosis and immunity-associated responses in various
plants. We have determined the crystal structure of an NLP from the
phytopathogenic oomycete Pythium aphanidermatum to 1.35A resolution. The protein
fold exhibits structural similarities to cytolytic toxins produced by marine
organisms (actinoporins). Computational modeling of the 3-dimensional structure
of NLPs from another oomycete, Phytophthora parasitica, and from the
phytopathogenic bacterium, Pectobacterium carotovorum, revealed a high extent of
fold conservation. Expression of the 2 oomycete NLPs in an nlp-deficient P.
carotovorum strain restored bacterial virulence, suggesting that NLPs of
prokaryotic and eukaryotic origins are orthologous proteins. NLP mutant protein
analyses revealed that identical structural properties were required to cause
plasma membrane permeabilization and cytolysis in plant cells, as well as to
restore bacterial virulence. In sum, NLPs are conserved virulence factors whose
taxonomic distribution is exceptional for microbial phytotoxins, and that
contribute to host infection by plasma membrane destruction and cytolysis. We
further show that NLP-mediated phytotoxicity and plant defense gene expression
share identical fold requirements, suggesting that toxin-mediated interference
with host integrity triggers plant immunity-associated responses.
Phytotoxin-induced cellular damage-associated activation of plant defenses is
reminiscent of microbial toxin-induced inflammasome activation in vertebrates
and may thus constitute another conserved element in animal and plant innate
immunity.
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Secondary reference #1
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Title
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Purification, Crystallization and preliminary X-Ray diffraction analysis of an oomycete-Derived nep1-Like protein.
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Authors
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B.Luberacki,
M.Weyand,
U.Seitz,
W.Koch,
C.Oecking,
C.Ottmann.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008,
64,
1178-1180.
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PubMed id
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