2gdt is a 1 chain structure with sequence from Sars coronavirus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.
Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.,Almeida MS, Johnson MA, Herrmann T, Geralt M, Wuthrich K J Virol. 2007 Apr;81(7):3151-61. Epub 2007 Jan 3. PMID:17202208[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Almeida MS, Johnson MA, 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. 2007 Apr;81(7):3151-61. Epub 2007 Jan 3. PMID:17202208 doi:JVI.01939-06
