2jzf

Protein Summary

This amino acid sequence from Sars coronavirus forms the central segment of the SARS-unique domain (SUD-M, for "middle of the SARS-unique domain") in 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, although the two proteins share only 5% sequence identity in the homologous sequence regions. SUD-M(527-651) also shows three-dimensional structure homology with several helicases and nucleoside triphosphate-binding proteins, but it does not contain the motifs of catalytic residues found in these structural homologues [Ref].  The Nudix fold type classification SCOP55811 is in agreement with these observations, suggesting 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]. See 2rnk entry for further details.

Ligand Summary

References