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PDBsum entry 6y9m

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protein ligands Protein-protein interface(s) links
Viral protein PDB id
6y9m

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
195 a.a.
Ligands
NAG-NAG ×6
NAG-NAG-BMA-FUC
NAG-NAG-BMA
PO4 ×5
SO4
Waters ×7
PDB id:
6y9m
Name: Viral protein
Title: Crystal structure of tswv glycoprotein n ectodomain (sgn)
Structure: Glycoprotein. Chain: a, b, c, d. Engineered: yes
Source: Tomato spotted wilt virus (strain brazilian br- 01). Organism_taxid: 36413. Gene: gn, gc. Expressed in: trichoplusia ni. Expression_system_taxid: 7111
Resolution:
3.40Å     R-factor:   0.261     R-free:   0.283
Authors: M.Dessau,Y.Bahat
Key ref: Y.Bahat et al. (2020). Crystal structure of tomato spotted wilt virus GN reveals a dimer complex formation and evolutionary link to animal-infecting viruses. Proc Natl Acad Sci U S A, 117, 26237-26244. PubMed id: 33020295 DOI: 10.1073/pnas.2004657117
Date:
10-Mar-20     Release date:   30-Sep-20    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P36291  (GP_TSWV1) -  Envelopment polyprotein from Tomato spotted wilt virus (strain Brazilian Br-01)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1135 a.a.
195 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1073/pnas.2004657117 Proc Natl Acad Sci U S A 117:26237-26244 (2020)
PubMed id: 33020295  
 
 
Crystal structure of tomato spotted wilt virus GN reveals a dimer complex formation and evolutionary link to animal-infecting viruses.
Y.Bahat, J.Alter, M.Dessau.
 
  ABSTRACT  
 
Tospoviridae is a family of enveloped RNA plant viruses that infect many field crops, inflicting a heavy global economic burden. These tripartite, single-stranded, negative-sense RNA viruses are transmitted from plant to plant by thrips as the insect vector. The medium (M) segment of the viral genome encodes two envelope glycoproteins, GN and GC, which together form the envelope spikes. GC is considered the virus fusogen, while the accompanying GN protein serves as an attachment protein that binds to a yet unknown receptor, mediating the virus acquisition by the thrips carrier. Here we present the crystal structure of glycoprotein N (GN) from the tomato spotted wilt virus (TSWV), a representative member of the Tospoviridae family. The structure suggests that GN is organized as dimers on TSWV's outer shell. Our structural data also suggest that this dimerization is required for maintaining GN structural integrity. Although the structure of the TSWV GN is different from other bunyavirus GN proteins, they all share similar domain connectivity that resembles glycoproteins from unrelated animal-infecting viruses, suggesting a common ancestor for these accompanying proteins.
 

 

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