Novel β-Barrel Fold in the Nuclear Magnetic Resonance Structure of the Replicase Nonstructural Protein 1 from the Severe Acute Respiratory Syndrome Coronavirus
Novel β-Barrel Fold in the Nuclear Magnetic Resonance Structure of the Replicase Nonstructural Protein 1 from the Severe Acute Respiratory Syndrome Coronavirus
ABSTRACT 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 α/β-fold formed by a mixed parallel/antiparallel six-stranded β-barrel, an α-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.
- ETH Zurich Switzerland
- Institute of Molecular Biology and Biophysics Switzerland
- Scripps Research Institute United States
- Joint Center for Structural Genomics United States
Models, Molecular, Protein Folding, Molecular Sequence Data, Immunology, Viral Nonstructural Proteins, RNA-Dependent RNA Polymerase, Microbiology, Peptide Fragments, Protein Structure, Secondary, Recombinant Proteins, Protein Structure, Tertiary, Severe acute respiratory syndrome-related coronavirus, Insect Science, Virology, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular
Models, Molecular, Protein Folding, Molecular Sequence Data, Immunology, Viral Nonstructural Proteins, RNA-Dependent RNA Polymerase, Microbiology, Peptide Fragments, Protein Structure, Secondary, Recombinant Proteins, Protein Structure, Tertiary, Severe acute respiratory syndrome-related coronavirus, Insect Science, Virology, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular
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