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PDBsum entry 4zgh
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Sugar binding protein, toxin
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PDB id
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4zgh
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References listed in PDB file
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Key reference
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Title
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Crystal structure of streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.
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Authors
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S.L.Lawrence,
S.C.Feil,
C.J.Morton,
A.J.Farrand,
T.D.Mulhern,
M.A.Gorman,
K.R.Wade,
R.K.Tweten,
M.W.Parker.
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Ref.
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Sci Rep, 2015,
5,
14352.
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PubMed id
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Abstract
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Pore-forming proteins are weapons often used by bacterial pathogens to breach
the membrane barrier of target cells. Despite their critical role in infection
important structural aspects of the mechanism of how these proteins assemble
into pores remain unknown. Streptococcus pneumoniae is the world's leading cause
of pneumonia, meningitis, bacteremia and otitis media. Pneumolysin (PLY) is a
major virulence factor of S. pneumoniae and a target for both small molecule
drug development and vaccines. PLY is a member of the cholesterol-dependent
cytolysins (CDCs), a family of pore-forming toxins that form gigantic pores in
cell membranes. Here we present the structure of PLY determined by X-ray
crystallography and, in solution, by small-angle X-ray scattering. The crystal
structure reveals PLY assembles as a linear oligomer that provides key
structural insights into the poorly understood early monomer-monomer
interactions of CDCs at the membrane surface.
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