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2GRI

NMR Structure of the SARS-CoV non-structural protein nsp3a

Summary for 2GRI
Entry DOI10.2210/pdb2gri/pdb
NMR InformationBMRB: 7019
DescriptorNSP3 (1 entity in total)
Functional Keywordssars-cov, non-structural protein, nsp3, structural genomics, psi, protein structure initiative, joint center for structural genomics, jcsg, viral protein
Biological sourceSARS coronavirus
Total number of polymer chains1
Total formula weight12648.01
Authors
Primary citationSerrano, P.,Johnson, M.A.,Almeida, M.S.,Horst, R.,Herrmann, T.,Joseph, J.S.,Neuman, B.W.,Subramanian, V.,Saikatendu, K.S.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Wuthrich, K.
Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.
J.Virol., 81:12049-12060, 2007
Cited by
PubMed Abstract: This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.
PubMed: 17728234
DOI: 10.1128/JVI.00969-07
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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