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PDBsum entry 4ldb
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Viral protein
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PDB id
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4ldb
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Contents |
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266 a.a.
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249 a.a.
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237 a.a.
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235 a.a.
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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 rearrangement of ebola virus vp40 begets multiple functions in the virus life cycle.
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Authors
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Z.A.Bornholdt,
T.Noda,
D.M.Abelson,
P.Halfmann,
M.R.Wood,
Y.Kawaoka,
E.O.Saphire.
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Ref.
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Cell, 2013,
154,
763-774.
[DOI no: ]
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PubMed id
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Abstract
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Proteins, particularly viral proteins, can be multifunctional, but the
mechanisms behind multifunctionality are not fully understood. Here, we
illustrate through multiple crystal structures, biochemistry, and cellular
microscopy that VP40 rearranges into different structures, each with a distinct
function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer
traffics to the cellular membrane. Once there, electrostatic interactions
trigger rearrangement of the polypeptide into a linear hexamer. These hexamers
construct a multilayered, filamentous matrix structure that is critical for
budding and resembles tomograms of authentic virions. A third structure of VP40,
formed by a different rearrangement, is not involved in virus assembly but
instead uniquely binds RNA to regulate viral transcription inside infected
cells. These results provide a functional model for ebolavirus matrix assembly
and the other roles of VP40 in the virus life cycle and demonstrate how a single
wild-type, unmodified polypeptide can assemble into different structures for
different functions. PAPERFLICK:
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