4Z5V: Crystal Structure Of Mhv Ns2 Pde Domain

Prior studies have demonstrated that the mouse hepatitis virus (MHV) A59 strain ns2 protein is a member of the 2H phosphoesterase family and exhibits 2',5'-phosphodiesterase (PDE) activity. During the IFN antiviral response, ns2 cleaves 2',5'-oligoadenylate (2-5A), a key mediator of RNase L activation, thereby subverting the activation of RNase L and evading host innate immunity. However, the mechanism of 2-5A cleavage by ns2 remains unclear. Here, we present the crystal structure of the MHV ns2 PDE domain and demonstrate a PDE fold similar to that of the cellular protein, a kinase anchoring protein 7 central domain (AKAP7CD) and rotavirus VP3 carboxy-terminal domain. The structure displays a pair of strictly conserved HxT/Sx motifs and forms a deep, positively charged catalytic groove with beta-sheets and an arginine-containing loop. These findings provide insight into the structural basis for 2-5A binding of MHV ns2.
PDB ID: 4Z5VDownload
MMDB ID: 136368
PDB Deposition Date: 2015/4/3
Updated in MMDB: 2016/05
Experimental Method:
x-ray diffraction
Resolution: 3.05  Å
Source Organism:
Similar Structures:
Biological Unit for 4Z5V: dimeric; determined by author
Molecular Components in 4Z5V
Label Count Molecule
Proteins (2 molecules)
Non-structural Protein 2A
Molecule annotation
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Citing MMDB