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PDBsum entry 2wa2

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protein ligands Protein-protein interface(s) links
Transferase PDB id
2wa2
Jmol
Contents
Protein chains
223 a.a. *
259 a.a. *
Ligands
SAM ×2
SO4 ×3
Waters ×298
* Residue conservation analysis
PDB id:
2wa2
Name: Transferase
Title: Structure of the methyltransferase domain from modoc virus, a flavivirus with no known vector (nkv)
Structure: Non-structural protein 5. Chain: a, b. Fragment: ns5 protein, residues 2477-2744. Synonym: ns5 from modoc virus. Engineered: yes. Mutation: yes
Source: Modoc virus. Organism_taxid: 64300. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.80Å     R-factor:   0.188     R-free:   0.234
Authors: A.M.Jansson,P.Johansson,T.A.Jones
Key ref:
A.M.Jansson et al. (2009). Structure of the methyltransferase domain from the Modoc virus, a flavivirus with no known vector. Acta Crystallogr D Biol Crystallogr, 65, 796-803. PubMed id: 19622863 DOI: 10.1107/S0907444909017260
Date:
02-Feb-09     Release date:   04-Aug-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8QL64  (Q8QL64_9FLAV) -  Polyprotein
Seq:
Struc:
 
Seq:
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Seq:
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Seq:
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Seq:
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Seq:
Struc:
3374 a.a.
223 a.a.*
Protein chain
Pfam   ArchSchema ?
Q8QL64  (Q8QL64_9FLAV) -  Polyprotein
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
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Seq:
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Seq:
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Seq:
Struc:
3374 a.a.
259 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     methylation   1 term 
  Biochemical function     methyltransferase activity     3 terms  

 

 
DOI no: 10.1107/S0907444909017260 Acta Crystallogr D Biol Crystallogr 65:796-803 (2009)
PubMed id: 19622863  
 
 
Structure of the methyltransferase domain from the Modoc virus, a flavivirus with no known vector.
A.M.Jansson, E.Jakobsson, P.Johansson, V.Lantez, B.Coutard, X.de Lamballerie, T.Unge, T.A.Jones.
 
  ABSTRACT  
 
The Modoc virus (MODV) is a flavivirus with no known vector (NKV). Evolutionary studies have shown that the viruses in the MODV group have evolved in association with mammals (bats, rodents) without transmission by an arthropod vector. MODV methyltransferase is the first enzyme from this evolutionary branch to be structurally characterized. The high-resolution structure of the methyltransferase domain of the MODV NS5 protein (MTase(MODV)) was determined. The protein structure was solved in the apo form and in complex with its cofactor S-adenosyl-L-methionine (SAM). Although it belongs to a separate evolutionary branch, MTase(MODV) shares structural characteristics with flaviviral MTases from the other branches. Its capping machinery is a relatively new target in flaviviral drug development and the observed structural conservation between the three flaviviral branches indicates that it may be possible to identify a drug that targets a range of flaviviruses. The structural conservation also supports the choice of MODV as a possible model for flavivirus studies.
 
  Selected figure(s)  
 
Figure 3.
Figure 3 A superimposition of MTase[MODV] with MTases from DENV, MVEV, WNV (belonging to the mosquito-borne branch) and Meaban virus (from the tick-borne branch). Most stabilizing residues are conserved and the active sites from all three lineages align very well.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2009, 65, 796-803) copyright 2009.  
  Figure was selected by the author.