Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix
The viral Protein Kinase-1 (PK-1) phosphorylates the regulatory protein p6.9, which facilitates baculoviral genome release. Here, the authors combine X-ray crystallography with biophysical and biochemical analyses as well as molecular dynamics simulations to characterize Cydia pomenella granulovirus...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-21191-7 |
| _version_ | 1819127038467899392 |
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| author | Michael R. Oliver Christopher R. Horne Safal Shrestha Jeremy R. Keown Lung-Yu Liang Samuel N. Young Jarrod J. Sandow Andrew I. Webb David C. Goldstone Isabelle S. Lucet Natarajan Kannan Peter Metcalf James M. Murphy |
| author_facet | Michael R. Oliver Christopher R. Horne Safal Shrestha Jeremy R. Keown Lung-Yu Liang Samuel N. Young Jarrod J. Sandow Andrew I. Webb David C. Goldstone Isabelle S. Lucet Natarajan Kannan Peter Metcalf James M. Murphy |
| author_sort | Michael R. Oliver |
| collection | DOAJ |
| description | The viral Protein Kinase-1 (PK-1) phosphorylates the regulatory protein p6.9, which facilitates baculoviral genome release. Here, the authors combine X-ray crystallography with biophysical and biochemical analyses as well as molecular dynamics simulations to characterize Cydia pomenella granulovirus PK-1, which forms a dimer with a parallel side-to-side arrangement of the kinase domains and furthermore, they provide insights into its catalytic mechanism and evolutionary relationships with other kinases. |
| first_indexed | 2024-12-22T08:05:34Z |
| format | Article |
| id | doaj.art-68962591ebc346e3865840990c4f686b |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-22T08:05:34Z |
| publishDate | 2021-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-68962591ebc346e3865840990c4f686b2022-12-21T18:33:08ZengNature PortfolioNature Communications2041-17232021-02-0112111110.1038/s41467-021-21191-7Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helixMichael R. Oliver0Christopher R. Horne1Safal Shrestha2Jeremy R. Keown3Lung-Yu Liang4Samuel N. Young5Jarrod J. Sandow6Andrew I. Webb7David C. Goldstone8Isabelle S. Lucet9Natarajan Kannan10Peter Metcalf11James M. Murphy12School of Biological Sciences, University of AucklandWalter and Eliza Hall Institute of Medical ResearchInstitute of Bioinformatics, University of GeorgiaSchool of Biological Sciences, University of AucklandWalter and Eliza Hall Institute of Medical ResearchWalter and Eliza Hall Institute of Medical ResearchWalter and Eliza Hall Institute of Medical ResearchWalter and Eliza Hall Institute of Medical ResearchSchool of Biological Sciences, University of AucklandWalter and Eliza Hall Institute of Medical ResearchInstitute of Bioinformatics, University of GeorgiaSchool of Biological Sciences, University of AucklandWalter and Eliza Hall Institute of Medical ResearchThe viral Protein Kinase-1 (PK-1) phosphorylates the regulatory protein p6.9, which facilitates baculoviral genome release. Here, the authors combine X-ray crystallography with biophysical and biochemical analyses as well as molecular dynamics simulations to characterize Cydia pomenella granulovirus PK-1, which forms a dimer with a parallel side-to-side arrangement of the kinase domains and furthermore, they provide insights into its catalytic mechanism and evolutionary relationships with other kinases.https://doi.org/10.1038/s41467-021-21191-7 |
| spellingShingle | Michael R. Oliver Christopher R. Horne Safal Shrestha Jeremy R. Keown Lung-Yu Liang Samuel N. Young Jarrod J. Sandow Andrew I. Webb David C. Goldstone Isabelle S. Lucet Natarajan Kannan Peter Metcalf James M. Murphy Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix Nature Communications |
| title | Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_full | Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_fullStr | Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_full_unstemmed | Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_short | Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix |
| title_sort | granulovirus pk 1 kinase activity relies on a side to side dimerization mode centered on the regulatory αc helix |
| url | https://doi.org/10.1038/s41467-021-21191-7 |
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