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PDBsum entry 3gpq
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Viral protein/RNA
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PDB id
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3gpq
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Contents |
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160 a.a.
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150 a.a.
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148 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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The crystal structures of chikungunya and venezuelan equine encephalitis virus nsp3 macro domains define a conserved adenosine binding pocket.
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Authors
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H.Malet,
B.Coutard,
S.Jamal,
H.Dutartre,
N.Papageorgiou,
M.Neuvonen,
T.Ahola,
N.Forrester,
E.A.Gould,
D.Lafitte,
F.Ferron,
J.Lescar,
A.E.Gorbalenya,
X.De lamballerie,
B.Canard.
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Ref.
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J Virol, 2009,
83,
6534-6545.
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PubMed id
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Abstract
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Macro domains (also called "X domains") constitute a protein module family
present in all kingdoms of life, including viruses of the Coronaviridae and
Togaviridae families. Crystal structures of the macro domain from the
Chikungunya virus (an "Old World" alphavirus) and the Venezuelan equine
encephalitis virus (a "New World" alphavirus) were determined at resolutions of
1.65 and 2.30 A, respectively. These domains are active as adenosine
di-phosphoribose 1''-phosphate phosphatases. Both the Chikungunya and the
Venezuelan equine encephalitis virus macro domains are ADP-ribose binding
modules, as revealed by structural and functional analysis. A single aspartic
acid conserved through all macro domains is responsible for the specific binding
of the adenine base. Sequence-unspecific binding to long, negatively charged
polymers such as poly(ADP-ribose), DNA, and RNA is observed and attributed to
positively charged patches outside of the active site pocket, as judged by
mutagenesis and binding studies. The crystal structure of the Chikungunya virus
macro domain with an RNA trimer shows a binding mode utilizing the same
adenine-binding pocket as ADP-ribose, but avoiding the ADP-ribose 1''-phosphate
phosphatase active site. This leaves the AMP binding site as the sole common
feature in all macro domains.
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