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* Residue conservation analysis
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PDB id:
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Allergen
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Title:
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Solution structure of thE C-terminal domain ole e 9
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Structure:
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Beta-1,3-glucanase. Chain: a. Fragment: c-terminal domain. Engineered: yes
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Source:
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Olea europaea. Common olive. Organism_taxid: 4146. Gene: ole9. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
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NMR struc:
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20 models
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Authors:
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M.A.Trevino,O.Palomares,I.Castrillo,M.Villalba,R.Rodriguez, M.Rico,J.Santoro,M.Bruix
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Key ref:
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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:
DOI:
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Date:
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14-Mar-07
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Release date:
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29-Jan-08
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PROCHECK
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Headers
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References
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Q94G86
(Q94G86_OLEEU) -
Beta-1,3-glucanase-like protein
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Seq: Struc:
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460 a.a.
101 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Protein Sci
17:371-376
(2008)
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PubMed id:
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Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen.
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M.A.Treviño,
O.Palomares,
I.Castrillo,
M.Villalba,
R.Rodríguez,
M.Rico,
J.Santoro,
M.Bruix.
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ABSTRACT
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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.
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Selected figure(s)
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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
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2008,
17,
371-376)
copyright 2008.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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H.Chou,
M.F.Tam,
C.H.Chiang,
C.T.Chou,
H.Y.Tai,
and
H.D.Shen
(2011).
Transaldolases are novel and immunoglobulin E cross-reacting fungal allergens.
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Clin Exp Allergy, 41,
739-749.
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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.
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J Biol Chem, 284,
8461-8469.
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PDB codes:
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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.
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