4z5v

Publication Abstract from PubMed

Prior studies have demonstrated that the mouse hepatitis virus A59 strain (MHV-A59) ns2 protein is a member of the 2H phosphoesterase family and exhibits 2',5'-phosphodiesterase (2',5'-PDE) activity. During the interferon 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 (VP3-CTD). The structure displays a pair of strictly conserved HxS/Tx motifs and forms a deep positively charged catalytic groove with beta-sheets and an arginine containing loop (R-loop). These findings provide insight into the structural basis for 2-5A binding of MHV ns2.

Crystal structure of the mouse hepatitis virus ns2 phosphodiesterase domain that antagonizes RNase L activation.,Sui B, Huang J, Jha BK, Yin P, Zhou M, Fu ZF, Silverman RH, Weiss SR, Peng G, Zhao L J Gen Virol. 2016 Jan 12. doi: 10.1099/jgv.0.000395. PMID:26757803^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.