3IZX

3.1 Angstrom cryoEM structure of cytoplasmic polyhedrosis virus

Summary for 3IZX

• Entry DOI: 10.2210/pdb3izx/pdb
• EMDB information: 5256
• Descriptor: Structural protein VP3, Capsid protein VP1, Viral structural protein 5 (3 entities in total)
• Functional Keywords: cytoplasmic polyhedrosis virus, 3d reconstruction, cryoem, full atom model, virus
• Biological source: Bombyx mori cypovirus 1; More
• Total number of polymer chains: 5
• Total formula weight: 517125.94

Authors

Yu, X.,Ge, P.,Jiang, J.,Atanasov, I.,Zhou, Z.H. (deposition date: 2011-01-15, release date: 2011-06-22, Last modification date: 2024-10-16)

Primary citation

Yu, X.,Ge, P.,Jiang, J.,Atanasov, I.,Zhou, Z.H.
Atomic Model of CPV Reveals the Mechanism Used by This Single-Shelled Virus to Economically Carry Out Functions Conserved in Multishelled Reoviruses.
Structure, 19:652-661, 2011

PubMed Abstract: Unlike the multishelled viruses in the Reoviridae, cytoplasmic polyhedrosis virus (CPV) is single shelled, yet stable and fully capable of carrying out functions conserved within Reoviridae. Here, we report a 3.1 Å resolution cryo electron microscopy structure of CPV and derive its atomic model, consisting of 60 turret proteins (TPs), 120 each of capsid shell proteins (CSPs) and large protrusion proteins (LPPs). Two unique segments of CSP contribute to CPV's stability: an inserted protrusion domain interacting with neighboring proteins, and an N-anchor tying up CSPs together through strong interactions such as β sheet augmentation. Without the need to interact with outer shell proteins, LPP retains only the N-terminal two-third region containing a conserved helix-barrel core and interacts exclusively with CSP. TP is also simplified, containing only domains involved in RNA capping. Our results illustrate how CPV proteins have evolved in a coordinative manner to economically carry out their conserved functions.

PubMed: 21565700
DOI: 10.1016/j.str.2011.03.003

Experimental method

ELECTRON MICROSCOPY (3.1 Å)