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PDBsum entry 5msh

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protein Protein-protein interface(s) links
Virus PDB id
5msh

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
182 a.a.
369 a.a.
PDB id:
5msh
Name: Virus
Title: Cowpea mosaic virus top component (cpmv-t) - naturally occurring empty particles
Structure: Cowpea mosaic virus small subunit. Chain: a. Synonym: genome polyprotein m,p2. Engineered: yes. Cowpea mosaic virus large subunit. Chain: b. Synonym: genome polyprotein m,p2. Engineered: yes
Source: Cowpea mosaic virus. Cpmv. Organism_taxid: 12264. Strain: sb. Expressed in: nicotiana benthamiana. Expression_system_taxid: 4100. Expression_system_taxid: 4100
Authors: E.L.Hesketh,Y.Meshcheriakova,R.F.Thompson,G.P.Lomonossoff,N.A.Ranson
Key ref: E.L.Hesketh et al. (2017). The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy. Sci Rep, 7, 539. PubMed id: 28373698
Date:
04-Jan-17     Release date:   19-Jul-17    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P03599  (POL2_CPMVS) -  RNA2 polyprotein from Cowpea mosaic virus (strain SB)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1046 a.a.
182 a.a.
Protein chain
Pfam   ArchSchema ?
P03599  (POL2_CPMVS) -  RNA2 polyprotein from Cowpea mosaic virus (strain SB)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1046 a.a.
369 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Sci Rep 7:539 (2017)
PubMed id: 28373698  
 
 
The structures of a naturally empty cowpea mosaic virus particle and its genome-containing counterpart by cryo-electron microscopy.
E.L.Hesketh, Y.Meshcheriakova, R.F.Thompson, G.P.Lomonossoff, N.A.Ranson.
 
  ABSTRACT  
 
Cowpea mosaic virus (CPMV) is a picorna-like plant virus. As well as an intrinsic interest in CPMV as a plant pathogen, CPMV is of major interest in biotechnology applications such as nanotechnology. Here, we report high resolution cryo electron microscopy (cryo-EM) maps of wild type CPMV containing RNA-2, and of naturally-formed empty CPMV capsids. The resolution of these structures is sufficient to visualise large amino acids. We have refined an atomic model for each map and identified an essential amino acid involved in genome encapsidation. This work has furthered our knowledge of Picornavirales genome encapsidation and will assist further work in the development of CPMV as a biotechnological tool.
 

 

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