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PDBsum entry 4xal
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Viral protein
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PDB id
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4xal
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References listed in PDB file
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Key reference
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Title
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Vp22 core domain from herpes simplex virus 1 reveals a surprising structural conservation in both the alpha- And gammaherpesvirinae subfamilies.
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Authors
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K.Hew,
S.L.Dahlroth,
L.X.Pan,
T.Cornvik,
P.Nordlund.
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Ref.
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J Gen Virol, 2015,
96,
1436-1445.
[DOI no: ]
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PubMed id
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Abstract
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The viral tegument is a layer of proteins between the herpesvirus capsid and its
outer envelope. According to phylogenetic studies, only a third of these
proteins are conserved amongst the three subfamilies (Alpha-, Beta- and
Gammaherpesvirinae) of the family Herpesviridae. Although some of these tegument
proteins have been studied in more detail, the structure and function of the
majority of them are still poorly characterized. VP22 from Herpes simplex virus
1 (subfamily Alphaherpesvirinae) is a highly interacting tegument protein that
has been associated with tegument assembly. We have determined the crystal
structure of the conserved core domain of VP22, which reveals an elongated dimer
with several potential protein-protein interaction regions and a peptide-binding
site. The structure provides us with the structural basics to understand the
numerous functional mutagenesis studies of VP22 found in the literature. It also
establishes an unexpected structural homology to the tegument protein ORF52 from
Murid herpesvirus 68 (subfamily Gammaherpesvirinae). Homologues for both VP22
and ORF52 have been identified in their respective subfamilies. Although there
is no obvious sequence overlap in the two subfamilies, this structural
conservation provides compelling structural evidence for shared ancestry and
functional conservation.
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