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PDBsum entry 2wql

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protein ligands metals Protein-protein interface(s) links
Allergen PDB id
2wql
Jmol
Contents
Protein chains
152 a.a. *
Ligands
P4C ×4
PEG ×6
Metals
_CL ×16
Waters ×16
* Residue conservation analysis
PDB id:
2wql
Name: Allergen
Title: Crystal structure of the major carrot allergen dau c 1
Structure: Major allergen dau c 1. Chain: a, b, c, d. Synonym: cr16, pathogenesis-related protein gea20. Engineered: yes. Mutation: yes
Source: Daucus carota. Carrot. Organism_taxid: 4039. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.70Å     R-factor:   0.222     R-free:   0.237
Authors: Z.Markovic-Housley,A.Basle,S.Padavattan,K.Hoffmann-Sommergru T.Schirmer
Key ref:
Z.Marković-Housley et al. (2009). Structure of the major carrot allergen Dau c 1. Acta Crystallogr D Biol Crystallogr, 65, 1206-1212. PubMed id: 19923716 DOI: 10.1107/S0907444909034854
Date:
24-Aug-09     Release date:   01-Sep-09    
Supersedes: 2vjg
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O04298  (DAU1_DAUCA) -  Major allergen Dau c 1
Seq:
Struc:
154 a.a.
152 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     response to biotic stimulus   2 terms 

 

 
DOI no: 10.1107/S0907444909034854 Acta Crystallogr D Biol Crystallogr 65:1206-1212 (2009)
PubMed id: 19923716  
 
 
Structure of the major carrot allergen Dau c 1.
Z.Marković-Housley, A.Basle, S.Padavattan, B.Maderegger, T.Schirmer, K.Hoffmann-Sommergruber.
 
  ABSTRACT  
 
Dau c 1 is a major allergen of carrot (Daucus carota) which displays IgE cross-reactivity with the homologous major birch-pollen allergen Bet v 1. The crystal structure of Dau c 1 has been determined to a resolution of 2.7 A, revealing tight dimers. The structure of Dau c 1 is similar to those of the major allergens from celery, Api g 1, and birch pollen, Bet v 1. Electron density has been observed in the hydrophobic cavity of each monomer and has been modelled with polyethylene glycol oligomers of varying length. Comparison of the surface topology and physicochemical properties of Dau c 1 and Bet v 1 revealed that they may have some, but not all, epitopes in common. This is in agreement with the observation that the majority of carrot-allergic patients have Bet v 1 cross-reactive IgE antibodies, whereas others have Dau c 1-specific IgE antibodies which do not recognize Bet v 1.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Schematic view of the Dau c 1 dimer with residual density (F[o] - F[c] map) contoured at 2.8 . The four monomers, A-D, associate into two virtually identical dimers AB (gold and green) and CD (not shown). The additional electron density observed in the hydrophobic cavity of each monomer was tentatively modelled with molecules of polyethylene glycol. The view in (b) is rotated around the horizontal axis by 90° with respect to the view in (a).
Figure 3.
Figure 3 Solvent-accessible surfaces of Dau c 1, Api g 1 and Bet v 1 viewed as in Fig. 2-(a) and the rear view with molecules rotated by 180° around the y axis (bottom row). Cyan colour denotes residues that are conserved between Dau c 1 and Api g 1 (left) and between Dau c 1 and Bet v 1 (right). Non-identical residues are shown in grey.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2009, 65, 1206-1212) copyright 2009.  
  Figures were selected by an automated process.