PDBsum entry: 1ss3

Allergen

PDB id: 1ss3

Contents

Protein chain

50 a.a.

PDB id:

1ss3

Name:

Allergen

Title:

Solution structure of ole e 6, an allergen from olive tree pollen

Structure:

Pollen allergen ole e 6. Chain: a. Engineered: yes

Source:

Olea europaea. Common olive. Organism_taxid: 4146. Gene: ole6. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

NMR struc:

25 models

Authors:

M.A.Trevino,M.F.Garcia-Mayoral,P.Barral,M.Villalba, J.Santoro,M.Rico,R.Rodriguez,M.Bruix

Key ref:

M.A.Treviño et al. (2004). NMR solution structure of Ole e 6, a major allergen from olive tree pollen. J Biol Chem, 279, 39035-39041. PubMed id: 15247256 DOI: 10.1074/jbc.M406045200

Date:

23-Mar-04 Release date: 03-Aug-04

Protein chain

O24172  (ALL6_OLEEU) -  Pollen allergen Ole e 6

Seq: 50 a.a.

Struc: 50 a.a.

DOI no: 10.1074/jbc.M406045200

J Biol Chem 279:39035-39041 (2004)

PubMed id: 15247256

NMR solution structure of Ole e 6, a major allergen from olive tree pollen.

M.A.Treviño, M.F.García-Mayoral, P.Barral, M.Villalba, J.Santoro, M.Rico, R.Rodríguez, M.Bruix.

ABSTRACT

Ole e 6 is a pollen protein from the olive tree (Olea europaea) that exhibits allergenic activity with a high prevalence among olive-allergic individuals. The three-dimensional structure of Ole e 6 has been determined in solution by NMR methods. This is the first experimentally determined structure of an olive tree pollen allergen. The structure of this 50-residue protein is based on 486 upper limit distance constraints derived from nuclear Overhauser effects and 24 torsion angle restraints. The global fold of Ole e 6 consists of two nearly antiparallel alpha-helices, spanning residues 3-19 and 23-33, that are connected by a short loop and followed by a long, unstructured C-terminal tail. Viewed edge-on, the structured N terminus has a dumbbell-like shape with the two helices on the outside and with the hydrophobic core, mainly composed of 3 aromatic and 6 cysteine residues, on the inside. All the aromatic rings lie on top of and pack against the three disulfide bonds. The lack of thermal unfolding, even at 85 degrees C, indicates a high conformational stability. Based on the analysis of the molecular surface, we propose five plausible epitopes for IgE recognition. The results presented here provide the structural foundation for future experiments to verify the antigenicity of the proposed epitopes, as well as to design novel hypoallergenic forms of the protein suitable for diagnosis and treatment of type-I allergies. In addition, three-dimensional structure features of Ole e 6 are discussed to provide a basis for future functional studies.

Selected figure(s)

Figure 3.
FIG. 3. Details of the solution structure of Ole e 6. A, superposition of 25 conformers. Helix I is colored in blue, helix II in green, the loop between helices in yellow, the N-terminal end in magenta, and the unstructured C terminus in gray. B, electrostatic surface. Positive areas are represented in blue, and negative areas are represented in red. C, ribbon diagram colored as in A. A, B, and C were produced with MOLMOL.

Figure 4.
FIG. 4. Stereoscopic representation of the protein core of Ole e 6. The backbone atoms are in gray, and the aromatic groups and the disulfide bonds are in black.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2004, 279, 39035-39041) copyright 2004.

Figures were selected by the author.