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PDBsum entry 2jzf
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Viral protein
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PDB id
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2jzf
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References listed in PDB file
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Key reference
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Title
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Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-Unique domain contains a macrodomain fold.
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Authors
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A.Chatterjee,
M.A.Johnson,
P.Serrano,
B.Pedrini,
J.S.Joseph,
B.W.Neuman,
K.Saikatendu,
M.J.Buchmeier,
P.Kuhn,
K.Wüthrich.
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Ref.
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J Virol, 2009,
83,
1823-1836.
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PubMed id
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Abstract
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The nuclear magnetic resonance (NMR) structure of a central segment of the
previously annotated severe acute respiratory syndrome (SARS)-unique domain
(SUD-M, for "middle of the SARS-unique domain") in SARS coronavirus (SARS-CoV)
nonstructural protein 3 (nsp3) has been determined. SUD-M(513-651) exhibits a
macrodomain fold containing the nsp3 residues 528 to 648, and there is a
flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal
flexible tail of residues 649 to 651. As a follow-up to this initial result, we
also solved the structure of a construct representing only the globular domain
of residues 527 to 651 [SUD-M(527-651)]. NMR chemical shift perturbation
experiments showed that SUD-M(527-651) binds single-stranded poly(A) and
identified the contact area with this RNA on the protein surface, and
electrophoretic mobility shift assays then confirmed that SUD-M has higher
affinity for purine bases than for pyrimidine bases. In a further search for
clues to the function, we found that SUD-M(527-651) has the closest
three-dimensional structure homology with another domain of nsp3, the
ADP-ribose-1"-phosphatase nsp3b, although the two proteins share only 5%
sequence identity in the homologous sequence regions. SUD-M(527-651) also shows
three-dimensional structure homology with several helicases and nucleoside
triphosphate-binding proteins, but it does not contain the motifs of catalytic
residues found in these structural homologues. The combined results from NMR
screening of potential substrates and the structure-based homology studies now
form a basis for more focused investigations on the role of the SARS-unique
domain in viral infection.
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