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<jats:p>Many viral genomes encode kinase and phosphatase enzymes to manipulate pathways that are controlled by phosphorylation events. The majority of viral phosphatase genes occur in the <jats:italic>Baculoviridae</jats:italic> and <jats:italic>Poxviridae</jats:italic> families of large DNA viruses. The corresponding protein sequences belong to four major homology groups, and structures are currently available for only two of these. Here, the first structure from the third group, the protein tyrosine phosphatase-2 (PTP-2) class of viral phosphatases, is described. It is shown that <jats:italic>Cydia pomonella</jats:italic> granulovirus PTP-2 has the same general fold and active-site architecture as described previously for other phosphatases, in the absence of significant sequence homology. Additionally, it has a novel C-terminal extension in an area corresponding to the interface of dimeric poxvirus phosphatases belonging to the Tyr–Ser protein phosphatase homology group.</jats:p>

Original publication




Journal article


Acta Crystallographica Section F Structural Biology Communications


International Union of Crystallography (IUCr)

Publication Date





233 - 238