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PDBsum entry 3vtt

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protein ligands Protein-protein interface(s) links
Viral protein, structural protein PDB id
3vtt

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
100 a.a.
Ligands
SO4 ×2
Waters ×146
PDB id:
3vtt
Name: Viral protein, structural protein
Title: High resolution crystal structure of dengue 3 envelope protein domain iii (ed3)
Structure: Envelope protein e. Chain: a, b. Fragment: unp residues 574-678. Engineered: yes
Source: Dengue virus type 3. Denv-3. Organism_taxid: 408870. Strain: philippines/h87/1956. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.208     R-free:   0.255
Authors: M.Elahi,M.M.Islam,Y.Kuroda
Key ref: M.Elahi et al. (2013). High resolution crystal structure of dengue-3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition. Proteins, 81, 1090-1095. PubMed id: 23239402 DOI: 10.1002/prot.24237
Date:
07-Jun-12     Release date:   26-Dec-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P27915  (POLG_DEN3P) -  Genome polyprotein from Dengue virus type 3 (strain Philippines/H87/1956)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
3390 a.a.
100 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.2.1.1.56  - mRNA (guanine-N(7))-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA
+ S-adenosyl-L- methionine
= 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA
+ S-adenosyl-L-homocysteine
   Enzyme class 2: E.C.2.1.1.57  - methyltransferase cap1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)- (2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H+
5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA
+ S-adenosyl-L-methionine
= 5'-end (N(7)-methyl 5'-triphosphoguanosine)- (2'-O-methyl-ribonucleoside) in mRNA
+ S-adenosyl-L-homocysteine
+ H(+)
   Enzyme class 3: E.C.2.7.7.48  - RNA-directed Rna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
RNA(n)
+ ribonucleoside 5'-triphosphate
= RNA(n+1)
+ diphosphate
   Enzyme class 4: E.C.3.4.21.91  - flavivirin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Selective hydrolysis of Xaa-Xaa-|-Xbb bonds in which each of the Xaa can be either Arg or Lys and Xbb can be either Ser or Ala.
   Enzyme class 5: E.C.3.6.1.15  - nucleoside-triphosphate phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
ribonucleoside 5'-triphosphate
+ H2O
= ribonucleoside 5'-diphosphate
+ phosphate
+ H(+)
   Enzyme class 6: E.C.3.6.4.13  - Rna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1002/prot.24237 Proteins 81:1090-1095 (2013)
PubMed id: 23239402  
 
 
High resolution crystal structure of dengue-3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition.
M.Elahi, M.M.Islam, K.Noguchi, M.Yohda, Y.Kuroda.
 
  ABSTRACT  
 
Dengue viruses are classified into four serotypes. Here, we report a 1.7 Å crystal structure of a recombinant dengue-3 envelope protein domain III (ED3), which contains most of the putative epitopes. Although the fold was well conserved, we found that a local backbone deformation in the first β-strand, which contains the putative epitope-1, occurred upon domain isolation. Furthermore, a comparison with dengue-2 ED3 indicated a large structural change by as much as 4.0 Å at Asp(662) , located in epitope-2. These minute structural and surface properties changes observed in the high resolution ED3 structure represent potential determinants for serospecificity and epitope recognition by antibodies. © 2012 Wiley Periodicals, Inc.
 

 

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