2GRI
NMR Structure of the SARS-CoV non-structural protein nsp3a
Summary for 2GRI
Entry DOI | 10.2210/pdb2gri/pdb |
NMR Information | BMRB: 7019 |
Descriptor | NSP3 (1 entity in total) |
Functional Keywords | sars-cov, non-structural protein, nsp3, structural genomics, psi, protein structure initiative, joint center for structural genomics, jcsg, viral protein |
Biological source | SARS coronavirus |
Total number of polymer chains | 1 |
Total formula weight | 12648.01 |
Authors | Serrano, P.,Almeida, M.S.,Johnson, M.A.,Herrmann, T.,Saikatendu, K.S.,Joseph, J.,Subramanian, V.,Neuman, B.W.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Wuthrich, K.,Joint Center for Structural Genomics (JCSG) (deposition date: 2006-04-24, release date: 2006-12-19, Last modification date: 2024-05-08) |
Primary citation | Serrano, 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: 17728234DOI: 10.1128/JVI.00969-07 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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