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PDBsum entry 2fav
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Viral protein
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PDB id
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2fav
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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 and functional basis for ADP-Ribose and poly(ADP-Ribose) binding by viral macro domains.
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Authors
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M.P.Egloff,
H.Malet,
A.Putics,
M.Heinonen,
H.Dutartre,
A.Frangeul,
A.Gruez,
V.Campanacci,
C.Cambillau,
J.Ziebuhr,
T.Ahola,
B.Canard.
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Ref.
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J Virol, 2006,
80,
8493-8502.
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PubMed id
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Abstract
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Macro domains constitute a protein module family found associated with specific
histones and proteins involved in chromatin metabolism. In addition, a small
number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and
hepatitis E virus, encode macro domains for which, however, structural and
functional information is extremely limited. Here, we characterized the macro
domains from hepatitis E virus, Semliki Forest virus, and severe acute
respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the
SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with
ADP-ribose. Information derived from structural, mutational, and sequence
analyses suggests a close phylogenetic and, most probably, functional
relationship between viral and cellular macro domain homologs. The data revealed
that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase
activities (which were previously proposed to be their biologically relevant
function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound
poly(ADP-ribose) in vitro. Collectively, these results suggest to further
evaluate the role of viral macro domains in host response to viral infection.
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Secondary reference #1
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Title
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Authors
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K.Dalle,
N.Bremond,
F.Tocque,
S.Blangy,
V.Campanacci,
B.Coutard,
S.Grisel,
J.Lichiere,
V.Lantez,
C.Cambillau.
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Ref.
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...
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