5A33

Electron cryo-microscopy of Cowpea Mosaic Virus (CPMV) empty virus like particle (eVLP)

Summary for 5A33

• Entry DOI: 10.2210/pdb5a33/pdb
• Related: 5A32
• EMDB information: 3014
• Descriptor: RNA2 POLYPROTEIN (2 entities in total)
• Functional Keywords: virus, cpmv, evlp, comoviridae, picornavirales.
• Biological source: COWPEA MOSAIC VIRUS (CPMV); More
• Cellular location: Movement protein: Host cell junction, host plasmodesma. Large coat protein: Virion : P03599 P03599
• Total number of polymer chains: 2
• Total formula weight: 64657.34

Authors

Hesketh, E.L.,Meshcheriakova, Y.,Dent, K.C.,Saxena, P.,Thompson, R.,Cockburn, J.J.,Lomonossoff, G.P.,Ranson, N.A. (deposition date: 2015-05-27, release date: 2015-12-23, Last modification date: 2024-05-08)

Primary citation

Hesketh, E.L.,Meshcheriakova, Y.,Dent, K.C.,Saxena, P.,Thompson, R.F.,Cockburn, J.J.,Lomonossoff, G.P.,Ranson, N.A.
Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM.
Nat Commun, 6:10113-10113, 2015

PubMed Abstract: Cowpea mosaic virus is a plant-infecting member of the Picornavirales and is of major interest in the development of biotechnology applications. Despite the availability of >100 crystal structures of Picornavirales capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 Å and 3.0 Å resolution, respectively, and built de novo atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which was missing from previously determined crystal structures, as well as residues that bind to the viral genome. These observations allow us to develop a new model for genome encapsidation and capsid assembly.

PubMed: 26657148
DOI: 10.1038/ncomms10113

Experimental method

ELECTRON MICROSCOPY (3.04 Å)