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8OPE

Virus-like Particle based on PVY coat protein with dC40 deletion with helical architecture encapsidating ssRNA

This is a non-PDB format compatible entry.
Summary for 8OPE
Entry DOI10.2210/pdb8ope/pdb
Related8OPD
EMDB information17049 17050
DescriptorGenome polyprotein (Fragment), RNA (5'-R(P*UP*UP*UP*UP*U)-3') (2 entities in total)
Functional Keywordshelical, dc40, vlp, ssrna, potyvirus, pvy, virus like particle
Biological sourcePotato virus Y strain NTN
More
Total number of polymer chains42
Total formula weight567984.31
Authors
Kavcic, L.,Kezar, A.,Podobnik, M. (deposition date: 2023-04-07, release date: 2024-01-24, Last modification date: 2024-01-31)
Primary citationKavcic, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.09 Å)
Structure validation

227344

數據於2024-11-13公開中

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