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Title
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Crystal structure of the matrix protein VP40 from Ebola virus.
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Authors
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A.Dessen,
V.Volchkov,
O.Dolnik,
H.D.Klenk,
W.Weissenhorn.
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Ref.
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EMBO J, 2000,
19,
4228-4236.
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PubMed id
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Abstract
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Ebola virus maturation occurs at the plasma membrane of infected cells and
involves the clustering of the viral matrix protein VP40 at the assembly site as
well as its interaction with the lipid bilayer. Here we report the X-ray crystal
structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure
reveals that Ebola virus VP40 is topologically distinct from all other known
viral matrix proteins, consisting of two domains with unique folds, connected by
a flexible linker. The C-terminal domain, which is absolutely required for
membrane binding, contains large hydrophobic patches that may be involved in the
interaction with lipid bilayers. Likewise, a highly basic region is shared
between the two domains. The crystal structure reveals how the molecule may be
able to switch from a monomeric conformation to a hexameric form, as observed in
vitro. Its implications for the assembly process are discussed.
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