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Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix
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Oliver, Michael R., Horne, Christopher R., Shrestha, Safal, Keown, Jeremy R., Liang, Lung-Yu, Young, Samuel N., Sandow, Jarrod J., Webb, Andrew I., Goldstone, David C., Lucet, Isabelle S., Kannan, Natarajan, Metcalf, Peter and Murphy, James M. (2021) Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix. Nature Communications, 12 (1). 1002. doi:10.1038/s41467-021-21191-7 ISSN 2041-1723.
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Official URL: http://doi.org/10.1038/s41467-021-21191-7
Abstract
The life cycle of Baculoviridae family insect viruses depends on the viral protein kinase, PK-1, to phosphorylate the regulatory protein, p6.9, to induce baculoviral genome release. Here, we report the crystal structure of Cydia pomenella granulovirus PK-1, which, owing to its likely ancestral origin among host cell AGC kinases, exhibits a eukaryotic protein kinase fold. PK-1 occurs as a rigid dimer, where an antiparallel arrangement of the αC helices at the dimer core stabilizes PK-1 in a closed, active conformation. Dimerization is facilitated by C-lobe:C-lobe and N-lobe:N-lobe interactions between protomers, including the domain-swapping of an N-terminal helix that crowns a contiguous β-sheet formed by the two N-lobes. PK-1 retains a dimeric conformation in solution, which is crucial for catalytic activity. Our studies raise the prospect that parallel, side-to-side dimeric arrangements that lock kinase domains in a catalytically-active conformation could function more broadly as a regulatory mechanism among eukaryotic protein kinases.
Item Type: | Journal Article | ||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||
Journal or Publication Title: | Nature Communications | ||||||
Publisher: | Nature Publishing Group | ||||||
ISSN: | 2041-1723 | ||||||
Official Date: | 12 February 2021 | ||||||
Dates: |
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Volume: | 12 | ||||||
Number: | 1 | ||||||
Article Number: | 1002 | ||||||
DOI: | 10.1038/s41467-021-21191-7 | ||||||
Status: | Peer Reviewed | ||||||
Publication Status: | Published | ||||||
Access rights to Published version: | Open Access (Creative Commons) |
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