Abstract
The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallography, X-Ray
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DNA, Single-Stranded / metabolism*
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Molecular Sequence Data
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Protein Structure, Tertiary
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RNA / metabolism*
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RNA-Binding Proteins / genetics*
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RNA-Binding Proteins / metabolism
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Sequence Analysis, Protein
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Severe Acute Respiratory Syndrome / metabolism*
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Severe Acute Respiratory Syndrome / virology
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Severe acute respiratory syndrome-related coronavirus / genetics*
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Severe acute respiratory syndrome-related coronavirus / metabolism
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Viral Proteins / genetics*
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Viral Proteins / metabolism
Substances
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DNA, Single-Stranded
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RNA-Binding Proteins
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Viral Proteins
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nsp9 protein, SARS virus
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RNA