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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

DOI

10.1107/s2053230x19002322

Type

Journal article

Journal

Acta Crystallographica Section F Structural Biology Communications

Publisher

International Union of Crystallography (IUCr)

Publication Date

01/04/2019

Volume

75

Pages

233 - 238