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2GDT

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

Summary for 2GDT
Entry DOI10.2210/pdb2gdt/pdb
NMR InformationBMRB: 7014
DescriptorLeader protein; p65 homolog; NSP1 (EC 3.4.22.-) (1 entity in total)
Functional Keywordsleader protein, beta-barrel, alpha-beta, virus, replicase, structural genomics, psi-2, protein structure initiative, joint center for structural genomics, jcsg, viral protein, hydrolase
Biological sourceSARS coronavirus
Total number of polymer chains1
Total formula weight12680.53
Authors
Primary citationAlmeida, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2024-10-30公开中

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