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PDBsum entry 5e8c
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Viral protein
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PDB id
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5e8c
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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 the herpesvirus nuclear egress complex provides insights into inner nuclear membrane remodeling.
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Authors
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T.Zeev-Ben-Mordehai,
M.Weberruß,
M.Lorenz,
J.Cheleski,
T.Hellberg,
C.Whittle,
K.El omari,
D.Vasishtan,
K.C.Dent,
K.Harlos,
K.Franzke,
C.Hagen,
B.G.Klupp,
W.Antonin,
T.C.Mettenleiter,
K.Grünewald.
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Ref.
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Cell Rep, 2015,
13,
2645-2652.
[DOI no: ]
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PubMed id
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Abstract
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Although nucleo-cytoplasmic transport is typically mediated through nuclear pore
complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway.
Together, the conserved herpesvirus proteins pUL31 and pUL34 form the
heterodimeric nuclear egress complex (NEC), which, in turn, mediates the
formation of tight-fitting membrane vesicles around capsids at the inner nuclear
membrane. Here, we present the crystal structure of the pseudorabies virus NEC.
The structure revealed that a zinc finger motif in pUL31 and an extensive
interaction network between the two proteins stabilize the complex.
Comprehensive mutational analyses, characterized both in situ and in vitro,
indicated that the interaction network is not redundant but rather
complementary. Fitting of the NEC crystal structure into the recently determined
cryoEM-derived hexagonal lattice, formed in situ by pUL31 and pUL34, provided
details on the molecular basis of NEC coat formation and inner nuclear membrane
remodeling.
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