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Allergen PDB-id
2jon
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Protein chain
101 a.a. *

* Residue conservation analysis
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PDB id: 2jon
Name: Allergen
Title: Solution structure of thE C-terminal domain ole e 9

Structure:
Beta-1,3-glucanase. Chain: a. Fragment: c-terminal domain. Engineered: yes

Source:
Olea europaea. Common olive. Organism_taxid: 4146. Gene: ole9. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

UniProt:
Q94G86 (Q94G86_OLEEU) Pfam   ArchSchema ?
Seq:
Struc:
Seq: 460 a.a.
Struc: 101 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Resolution:
not givenÅ

NMR structure:
20 models

Authors:
M.A.Trevino,O.Palomares,I.Castrillo,M.Villalba,R.Rodriguez, M.Rico,J.Santoro,M.Bruix

Key ref:
M.A.Treviño et al. (2008). Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen.. Protein Sci, 17, 371-376. [PubMed id: 18096638] [DOI: 10.1110/ps.073230008]

Date:
14-Mar-07

Release date:
29-Jan-08

Related entries:
7187 related db: bmrb
entry containing chemical shifts
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    Key reference    
 
 
DOI no: 10.1110/ps.073230008 Protein Sci 17:371-376 (2008)
PubMed id: 18096638  
 
 
Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen.
M.A.Treviño, O.Palomares, I.Castrillo, M.Villalba, R.Rodríguez, M.Rico, J.Santoro, M.Bruix.
 
  ABSTRACT  
 
Ole e 9 is an olive pollen allergen belonging to group 2 of pathogenesis-related proteins. The protein is composed of two immunological independent domains: an N-terminal domain (NtD) with 1,3-beta-glucanase activity, and a C-terminal domain (CtD) that binds 1,3-beta-glucans. We have determined the three-dimensional structure of CtD-Ole e 9 (101 amino acids), which consists of two parallel alpha-helices forming an angle of approximately 55 degrees , a small antiparallel beta-sheet with two short strands, and a 3-10 helix turn, all connected by long coil segments, resembling a novel type of folding among allergens. Two regions surrounded by aromatic residues (F49, Y60, F96, Y91 and Y31, H68, Y65, F78) have been localized on the protein surface, and a role for sugar binding is suggested. The epitope mapping of CtD-Ole e 9 shows that B-cell epitopes are mainly located on loops, although some of them are contained in secondary structural elements. Interestingly, the IgG and IgE epitopes are contiguous or overlapped, rather than coincident. The three-dimensional structure of CtD-Ole e 9 might help to understand the underlying mechanism of its biochemical function and to determine possible structure-allergenicity relationships.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. IgE and IgG epitopes of CtD-Ole e 9. (A) Location of the synthetic peptides used for the epitope mapping, in the CtD-Ole e
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2008, 17, 371-376) copyright 2008.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19097997 R.Hurtado-Guerrero, A.W.Schüttelkopf, I.Mouyna, A.F.Ibrahim, S.Shepherd, T.Fontaine, J.P.Latgé, and D.M.van Aalten (2009).
Molecular mechanisms of yeast cell wall glucan remodeling.
  J Biol Chem, 284, 8461-8469.
PDB codes: 2w61 2w62 2w63
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.