8OPK

Local refinement of cubic assembly from truncated PVY coat protein with K176C mutation

This is a non-PDB format compatible entry.

Summary for 8OPK

• Entry DOI: 10.2210/pdb8opk/pdb
• EMDB information: 17062 17063
• Descriptor: Genome polyprotein (1 entity in total)
• Functional Keywords: cubes, trcp, k176c, potyvirus, pvy, virus like particle
• Biological source: Potato virus Y strain NTN
• Total number of polymer chains: 16
• Total formula weight: 357766.78

Authors

Kavcic, L.,Kezar, A.,Podobnik, M. (deposition date: 2023-04-07, release date: 2024-01-24, Last modification date: 2024-01-31)

Primary citation

Kavcic, L.,Kezar, A.,Koritnik, N.,Znidaric, M.T.,Klobucar, T.,Vicic, Z.,Merzel, F.,Holden, E.,Benesch, J.L.P.,Podobnik, M.
From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y.
Commun Chem, 7:14-14, 2024

PubMed Abstract: The structural diversity and tunability of the capsid proteins (CPs) of various icosahedral and rod-shaped viruses have been well studied and exploited in the development of smart hybrid nanoparticles. However, the potential of CPs of the wide-spread flexuous filamentous plant viruses remains to be explored. Here, we show that we can control the shape, size, RNA encapsidation ability, symmetry, stability and surface functionalization of nanoparticles through structure-based design of CP from potato virus Y (PVY). We provide high-resolution insight into CP-based self-assemblies, ranging from large polymorphic or monomorphic filaments to smaller annular, cubic or spherical particles. Furthermore, we show that we can prevent CP self-assembly in bacteria by fusion with a cleavable protein, enabling controlled nanoparticle formation in vitro. Understanding the remarkable structural diversity of PVY CP not only provides possibilities for the production of biodegradable nanoparticles, but may also advance future studies of CP's polymorphism in a biological context.

PubMed: 38233506
DOI: 10.1038/s42004-024-01100-x

Experimental method

ELECTRON MICROSCOPY (3.16 Å)