The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3. Structure 13 1665-1675 2005
    Site JCSG
    PDB Id 2acf Target Id 367631
    Molecular Characteristics
    Source Sars coronavirus tor2
    Alias Ids TPS1517,29837497 Molecular Weight 18711.65 Da.
    Residues 175 Isoelectric Point 8.10
    Sequence pvnqftgylkltdnvaikcvdivkeaqsanpmvivnaanihlkhgggvagalnkatngamqkesddyik lngpltvggscllsghnlakkclhvvgpnlnagediqllkaayenfnsqdillapllsagifgakplqs lqvcvqtvrtqvyiavndkalyeqvvmdyldnlkprv
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 4
    Resolution (Å) 1.40 Rfree 0.18916
    Matthews' coefficent 2.60 Rfactor 0.16414
    Waters 950 Solvent Content 51.00

    Ligand Information


    Google Scholar output for 2acf
    1. Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1 _-phosphate dephosphorylation by a conserved domain of nsP3
    KS Saikatendu, JS Joseph, V Subramanian, T Clayton - Structure, 2005 - Elsevier
    2. The SARS-unique domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes
    J Tan, C Vonrhein, OS Smart, G Bricogne, M Bollati - PLoS , 2009 - dx.plos.org
    3. Crystal structures of the X_domains of a Group_1 and a Group_3 coronavirus reveal that ADP_ribose_binding may not be a conserved property
    Y Piotrowski, G Hansen - Protein , 2009 - Wiley Online Library
    4. 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
    5. The coronavirus replicase gene: special enzymes for special viruses
    J Ziebuhr, EJ Snijder - Coronavirusesmolecular and cellular , 2007 - books.google.com
    6. Viral enzymes
    JR Mesters, J Tan, R Hilgenfeld - Current opinion in structural biology, 2006 - Elsevier

    Protein Summary

    The gene 29837497 from Sars coronavirus encodes a conserved domain of nonstructural protein 3 (nsP3), a member of a macro family PF01661 SCOP52948.  The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ADP-ribose as a ligand. Previously identified as displaying an Appr-1"-p (ADP-ribose-1"-monophosphate) processing activity, the macro domain may play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation of proteins, an important post-translational modification which occurs in DNA repair, transcription, chromatin biology, and long-term memory formation, among other processes.  The SARS nsP3 domain readily removes the 1'' phosphate group from Appr-1''-p in in vitro assays, confirming its phosphatase activity [Ref]


    According to DALI, structurally similar proteins (Zscr=22) to 2acf/2fav are other viral RNA binding proteins like 3jzt, 3ew5, or 3eti.

    Ligand Summary





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