Crystal structure of protein tyrosine phosphatase‐2 from Cydia pomonella granulovirus. Issue 4 (5th April 2019)

• Record Type: Journal Article
• Authors: Huang, Guangmei; Oliver, Michael R.; Keown, Jeremy R.; Goldstone, David C.; Metcalf, Peter
• Is Part Of: Acta crystallographica. Volume 75:Issue 4(2019:Apr.)
• Page Start: 233
• Page End: 238
• Publication Date: 2019-04-05
• Subjects: Cydia pomonella granulovirus -- PTP‐2 -- protein tyrosine phosphatase‐2 -- phosphatases; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X19002322
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of the protein phosphatase PTP‐2 from Cydia pomonella granulovirus, a betabaculovirus, has been determined at 1.65 Å resolution. The structure shows that the molecule has a typical protein phosphatase fold with a unique β‐sheet extension at the C‐terminus. Abstract : 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 Baculoviridae and Poxviridae 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 Cydia pomonella 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.