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The Open Protein Structure Annotation Network
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2gri

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title 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
    Site JCSG
    PDB Id 2gri Target Id
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    Related PDB Ids 2idy 
    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1918,29837497
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method NMR
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    Chains 1

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2gri
    1. Structural proteomics of the SARS coronavirus: a model response to emerging infectious diseases
    M Bartlam, Y Xu, Z Rao - Journal of structural and functional genomics, 2007 - Springer
     
    2. Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus
    P Serrano, MA Johnson, MS Almeida, R Horst - Journal of , 2007 - Am Soc Microbiol
     

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    Protein Summary

     The gene 29837497 from SARS coronavirus encodes the N-terminal domain of nonstructural protein 3 (nsp3a).  The protein belongs to the class of alpha and beta proteins (a+b) and reveals beta-Grasp (ubiquitine-like) fold type SCOP.  The NMR structure of the same protein has been previously determined 2IDY.  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 new feature of this protein. NMR chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA [Ref].  The nsp3a homologue from rotovirus has been shown to bind to 3'-end of viral mRNA during viral infection [Ref].  While bound to mRNA nsp3a interacts with eukaryotic initiation factor 4GI (eIF4GI), displacing its normal partner PABP.  This interaction effectively shut offs the cellular protein synthesis, dedicating resources to the viral protein synthesis.  Thus, SARS nsp3a seems to have similar function.

    Ligand Summary



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