4IIS

Crystal structure of a glycosylated beta-1,3-glucanase (HEV B 2), An allergen from Hevea Brasiliensis (Space group P41)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.67 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 

wwPDB Validation   3D Report Full Report


This is version 3.1 of the entry. See complete history


Literature

Structural analysis of the endogenous glycoallergen Hev b 2 (endo-beta-1,3-glucanase) from Hevea brasiliensis and its recognition by human basophils.

Rodriguez-Romero, A.Hernandez-Santoyo, A.Fuentes-Silva, D.Palomares, L.A.Munoz-Cruz, S.Yepez-Mulia, L.Orozco-Martinez, S.

(2014) Acta Crystallogr D Biol Crystallogr 70: 329-341

  • DOI: https://doi.org/10.1107/S1399004713027673
  • Primary Citation of Related Structures:  
    4HPG, 4IIS

  • PubMed Abstract: 

    Endogenous glycosylated Hev b 2 (endo-β-1,3-glucanase) from Hevea brasiliensis is an important latex allergen that is recognized by IgE antibodies from patients who suffer from latex allergy. The carbohydrate moieties of Hev b 2 constitute a potentially important IgE-binding epitope that could be responsible for its cross-reactivity. Here, the structure of the endogenous isoform II of Hev b 2 that exhibits three post-translational modifications, including an N-terminal pyroglutamate and two glycosylation sites at Asn27 and at Asn314, is reported from two crystal polymorphs. These modifications form a patch on the surface of the molecule that is proposed to be one of the binding sites for IgE. A structure is also proposed for the most important N-glycan present in this protein as determined by digestion with specific enzymes. To analyze the role of the carbohydrate moieties in IgE antibody binding and in human basophil activation, the glycoallergen was enzymatically deglycosylated and evaluated. Time-lapse automated video microscopy of basophils stimulated with glycosylated Hev b 2 revealed basophil activation and degranulation. Immunological studies suggested that carbohydrates on Hev b 2 represent an allergenic IgE epitope. In addition, a dimer was found in each asymmetric unit that may reflect a regulatory mechanism of this plant defence protein.


  • Organizational Affiliation

    Instituto de Química, Universidad Nacional Autónoma de México, Circuito Exterior, CU, 04310 Coyoacán, DF, Mexico.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-1,3-glucanase form 'RRII Gln 2'
A, B, C, D
316Hevea brasiliensisMutation(s): 0 
EC: 3.2.1.39
UniProt
Find proteins for D1M8S7 (Hevea brasiliensis)
Explore D1M8S7 
Go to UniProtKB:  D1M8S7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupD1M8S7
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
E
2N-Glycosylation
Glycosylation Resources
GlyTouCan:  G42666HT
GlyCosmos:  G42666HT
GlyGen:  G42666HT
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.67 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 150.118α = 90
b = 150.118β = 90
c = 77.331γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
PHENIXrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-11-27
    Type: Initial release
  • Version 1.1: 2014-03-19
    Changes: Database references
  • Version 2.0: 2019-12-25
    Changes: Derived calculations, Polymer sequence
  • Version 3.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Atomic model, Data collection, Derived calculations, Structure summary
  • Version 3.1: 2023-09-20
    Changes: Data collection, Database references, Refinement description, Structure summary