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PDBsum entry 4zno
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Sugar binding protein
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PDB id
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4zno
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References listed in PDB file
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Key reference
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Title
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Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-Like protein.
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Authors
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N.Jia,
N.Liu,
W.Cheng,
Y.L.Jiang,
H.Sun,
L.L.Chen,
J.Peng,
Y.Zhang,
Y.H.Ding,
Z.H.Zhang,
X.Wang,
G.Cai,
J.Wang,
M.Q.Dong,
Z.Zhang,
H.Wu,
H.W.Wang,
Y.Chen,
C.Z.Zhou.
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Ref.
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Embo Rep, 2016,
17,
235-248.
[DOI no: ]
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PubMed id
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Abstract
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Various aerolysin-like pore-forming proteins have been identified from bacteria
to vertebrates. However, the mechanism of receptor recognition and/or pore
formation of the eukaryotic members remains unknown. Here, we present the first
crystal and electron microscopy structures of a vertebrate aerolysin-like
protein from Danio rerio, termed Dln1, before and after pore formation. Each
subunit of Dln1 dimer comprises a β-prism lectin module followed by an
aerolysin module. Specific binding of the lectin module toward high-mannose
glycans triggers drastic conformational changes of the aerolysin module in a
pH-dependent manner, ultimately resulting in the formation of a membrane-bound
octameric pore. Structural analyses combined with computational simulations and
biochemical assays suggest a pore-forming process with an activation mechanism
distinct from the previously characterized bacterial members. Moreover, Dln1 and
its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting
a novel fish-specific defense molecule.
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