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

    Title Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold. J.Virol. 83 1823-1836 2009
    Site JCSG
    PDB Id 2jze Target Id 391773
    Related PDB Ids 2jzd 
    Molecular Characteristics
    Source Sars coronavirus tor2
    Alias Ids TPS1786,29837497 Molecular Weight 13936.48 Da.
    Residues 125 Isoelectric Point 8.96
    Sequence gtvswnlremlahaeetrklmpicmdvraimatiqrkykgikiqegivdygvrfffytskepvasiitk lnslneplvtmpigyvthgfnleeaarcmrslkapavvsvsspdavttyngyltss
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information


    Google Scholar output for 2jze
    1. Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold
    A Chatterjee, MA Johnson, P Serrano, B Pedrini - Journal of , 2009 - Am Soc Microbiol

    Protein Summary

    The target 29837497 from Sars coronavirus encodes the central segment of SARS-unique domain (SUD-M, for "middle of the SARS-unique domain") of the nonstructural protein Nsp3 PF11633.  

    SUD-M(513-651) exhibits a macrodomain fold containing the Nsp3 residues 528 to 648, and there is a flexibly extended N-terminal tail with the residues 513 to 527 and a C-terminal flexible tail of residues 649 to 651.  NMR chemical shift perturbation experiments showed that SUD-M(527-651) binds single-stranded poly(A) RNA. SUD-M(527-651) has the closest three-dimensional structure homology with another domain of Nsp3, the ADP-ribose-1"-phosphatase Nsp3b (2kqv; DALI Z=20), although the two proteins share only 5% sequence identity in the homologous sequence regions. DALI returns a weak hit with the TTHA0132 protein 2dx6 (Z=10). SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins (PDB_ID: 3kh6; DALI Z=9), but it does not contain the motifs of catalytic residues found in these structural homologues [Ref].  

    The Nudix fold type classification from SCOP55811 is in agreement with these observations, suggesting a Nudix hydrolase-like functionality.  Nudix hydrolases are found in all classes of organisms and hydrolyse a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity [Ref]

    Ligand Summary





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