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PDBsum entry 2gdt
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Viral protein, hydrolase
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PDB id
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2gdt
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References listed in PDB file
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Key reference
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Title
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Novel beta-Barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
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Authors
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M.S.Almeida,
M.A.Johnson,
T.Herrmann,
M.Geralt,
K.Wüthrich.
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Ref.
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J Virol, 2007,
81,
3151-3161.
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PubMed id
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Abstract
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The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome
coronavirus has 179 residues and is the N-terminal cleavage product of the viral
replicase polyprotein that mediates RNA replication and processing. The specific
function of nsp1 is not known. Here we report the nuclear magnetic resonance
structure of the nsp1 segment from residue 13 to 128, which represents a novel
alpha/beta-fold formed by a mixed parallel/antiparallel six-stranded
beta-barrel, an alpha-helix covering one opening of the barrel, and a
3(10)-helix alongside the barrel. We further characterized the full-length
179-residue protein and show that the polypeptide segments of residues 1 to 12
and 129 to 179 are flexibly disordered. The structure is analyzed in a search
for possible correlations with the recently reported activity of nsp1 in the
degradation of mRNA.
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