2HSX

NMR Structure of the nonstructural protein 1 (nsp1) from the SARS coronavirus

Summary for 2HSX

• Entry DOI: 10.2210/pdb2hsx/pdb
• Related: 2gdt
• Descriptor: Leader protein; p65 homolog; NSP1 (EC 3.4.22.-) (1 entity in total)
• Functional Keywords: leader protein, beta-barrel, alpha-beta, virus, replicase, structural genomics, psi-2, protein structure initiative, joint center for structural genomics, jcsg, viral protein, hydrolase
• Biological source: SARS coronavirus
• Cellular location: Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P59641
• Total number of polymer chains: 1
• Total formula weight: 12680.53

Authors

Almeida, M.S.,Herrmann, T.,Geralt, M.,Johnson, M.A.,Saikatendu, K.,Joseph, J.,Subramanian, R.C.,Neuman, B.W.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Wilson, I.A.,Wuthrich, K.,Joint Center for Structural Genomics (JCSG) (deposition date: 2006-07-24, release date: 2007-02-06, Last modification date: 2024-05-29)

Primary citation

Almeida, M.S.,Johnson, M.A.,Herrmann, T.,Geralt, M.,Wuthrich, K.
Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
J.Virol., 81:3151-3161, 2007

PubMed 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 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.

PubMed: 17202208
DOI: 10.1128/JVI.01939-06

Experimental method

SOLUTION NMR