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PDBsum entry 2acf
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Viral protein
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PDB id
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2acf
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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 basis of severe acute respiratory syndrome coronavirus ADP-Ribose-1''-Phosphate dephosphorylation by a conserved domain of nsp3.
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Authors
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K.S.Saikatendu,
J.S.Joseph,
V.Subramanian,
T.Clayton,
M.Griffith,
K.Moy,
J.Velasquez,
B.W.Neuman,
M.J.Buchmeier,
R.C.Stevens,
P.Kuhn.
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Ref.
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Structure (Camb), 2005,
13,
1665-1675.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of a conserved domain of nonstructural protein 3 (nsP3)
from severe acute respiratory syndrome coronavirus (SARS-CoV) has been solved by
single-wavelength anomalous dispersion to 1.4 A resolution. The structure of
this "X" domain, seen in many single-stranded RNA viruses, reveals a
three-layered alpha/beta/alpha core with a macro-H2A-like fold. The putative
active site is a solvent-exposed cleft that is conserved in its three structural
homologs, yeast Ymx7, Archeoglobus fulgidus AF1521, and Er58 from E. coli. Its
sequence is similar to yeast YBR022W (also known as Poa1P), a known phosphatase
that acts on ADP-ribose-1''-phosphate (Appr-1''-p). The SARS nsP3 domain readily
removes the 1'' phosphate group from Appr-1''-p in in vitro assays, confirming
its phosphatase activity. Sequence and structure comparison of all known
macro-H2A domains combined with available functional data suggests that proteins
of this superfamily form an emerging group of nucleotide phosphatases that
dephosphorylate Appr-1''-p.
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Figure 2.
Figure 2. Structure of SARS ADRP
(A) Ribbon
representation of the SARS nsP3 ADRP monomer. The two
glycine-rich loops are shown in yellow. Secondary structures are
colored from blue (N) to red (C terminus). Helices are numbered
H1-H6, and b strands are numbered from 1 to 8.
(B) The SARS
ADRP dimer observed between the B and D subunits in the
asymmetric unit. The four conserved segments are colored red in
each subunit; the conserved histidines and asparagines at the
active site are shown as ball-and-sticks.
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The above figure is
reprinted
by permission from Cell Press:
Structure (Camb)
(2005,
13,
1665-1675)
copyright 2005.
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