3CNF

3.88 Angstrom structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy

Summary for 3CNF

• Entry DOI: 10.2210/pdb3cnf/pdb
• EMDB information: 1508
• Descriptor: VP1, VP3 (2 entities in total)
• Functional Keywords: cytoplasmic polyhedrosis virus, capsid protein, turret protein, polyhedrin-binding domain, guanylyltransferase domain, icosahedral virus, virus
• Biological source: Bombyx mori cypovirus 1; More
• Cellular location: Virion: Q6TS43
• Total number of polymer chains: 3
• Total formula weight: 416868.83

Authors

Yu, X.,Jin, L.,Zhou, Z.H. (deposition date: 2008-03-25, release date: 2008-04-29, Last modification date: 2024-02-21)

Primary citation

Yu, X.,Jin, L.,Zhou, Z.H.
3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy.
Nature, 453:415-419, 2008

PubMed Abstract: Cytoplasmic polyhedrosis virus (CPV) is unique within the Reoviridae family in having a turreted single-layer capsid contained within polyhedrin inclusion bodies, yet being fully capable of cell entry and endogenous RNA transcription. Biochemical data have shown that the amino-terminal 79 residues of the CPV turret protein (TP) is sufficient to bring CPV or engineered proteins into the polyhedrin matrix for micro-encapsulation. Here we report the three-dimensional structure of CPV at 3.88 A resolution using single-particle cryo-electron microscopy. Our map clearly shows the turns and deep grooves of alpha-helices, the strand separation in beta-sheets, and densities for loops and many bulky side chains; thus permitting atomic model-building effort from cryo-electron microscopy maps. We observed a helix-to-beta-hairpin conformational change between the two conformational states of the capsid shell protein in the region directly interacting with genomic RNA. We have also discovered a messenger RNA release hole coupled with the mRNA capping machinery unique to CPV. Furthermore, we have identified the polyhedrin-binding domain, a structure that has potential in nanobiotechnology applications.

PubMed: 18449192
DOI: 10.1038/nature06893

Experimental method

ELECTRON MICROSCOPY (3.88 Å)