6VVG
Structure of the Cydia pomonella Granulovirus kinase, PK-1
Summary for 6VVG
| Entry DOI | 10.2210/pdb6vvg/pdb |
| Descriptor | Arginine kinase, ADENOSINE MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | protein kinase, viral protein, kinase |
| Biological source | Cydia pomonella granulosis virus (isolate Mexican) (CpGV) |
| Total number of polymer chains | 2 |
| Total formula weight | 65917.03 |
| Authors | Oliver, M.R.,Horne, C.R.,Keown, J.R.,Murphy, J.M.,Metcalf, P. (deposition date: 2020-02-17, release date: 2021-02-03, Last modification date: 2023-10-11) |
| Primary citation | Oliver, M.R.,Horne, C.R.,Shrestha, S.,Keown, J.R.,Liang, L.Y.,Young, S.N.,Sandow, J.J.,Webb, A.I.,Goldstone, D.C.,Lucet, I.S.,Kannan, N.,Metcalf, P.,Murphy, J.M. Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory alpha C helix. Nat Commun, 12:1002-1002, 2021 Cited by PubMed 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. PubMed: 33579933DOI: 10.1038/s41467-021-21191-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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