6I28
Crystal Structure of Cydia Pomonella PTP-2 phosphatase
Summary for 6I28
| Entry DOI | 10.2210/pdb6i28/pdb |
| Descriptor | ORF98 PTP-2, GLYCEROL, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | cydia pomonella, ptp-2 phosphatase, viral protein |
| Biological source | Cydia pomonella granulosis virus (CpGV) |
| Total number of polymer chains | 1 |
| Total formula weight | 19610.48 |
| Authors | Huang, G.,Keown, J.P.,Oliver, M.R.,Metcalf, P. (deposition date: 2018-10-31, release date: 2019-02-20, Last modification date: 2024-05-15) |
| Primary citation | Huang, G.,Oliver, M.R.,Keown, J.R.,Goldstone, D.C.,Metcalf, P. Crystal structure of protein tyrosine phosphatase-2 from Cydia pomonella granulovirus. Acta Crystallogr.,Sect.F, 75:233-238, 2019 Cited by PubMed 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. PubMed: 30950823DOI: 10.1107/S2053230X19002322 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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