3cnf
From Proteopedia
3.88 Angstrom structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
Overview
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.
About this Structure
3CNF is a Protein complex structure of sequences from Bombyx mori cypovirus 1. Full crystallographic information is available from OCA.
Reference
3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy., Yu X, Jin L, Zhou ZH, Nature. 2008 May 15;453(7193):415-9. Epub 2008 Apr 30. PMID:18449192 Page seeded by OCA on Thu May 22 22:37:38 2008
