RCSB PDB - 4AGI: Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with seleno fucoside.

 4AGI

Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with seleno fucoside.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.185 
  • R-Value Work: 0.152 
  • R-Value Observed: 0.154 

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Ligand Structure Quality Assessment 

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Literature

A Soluble Fucose-Specific Lectin from Aspergillus Fumigatus Conidia - Structure, Specificity and Possible Role in Fungal Pathogenicity.

Houser, J.Komarek, J.Kostlanova, N.Cioci, G.Varrot, A.Kerr, S.C.Lahmann, M.Balloy, V.Fahy, J.V.Chignard, M.Imberty, A.Wimmerova, M.

(2013) PLoS One 8: 83077

  • DOI: https://doi.org/10.1371/journal.pone.0083077
  • Primary Citation of Related Structures:  
    4AGI

  • PubMed Abstract: 

    Aspergillus fumigatus is an important allergen and opportunistic pathogen. Similarly to many other pathogens, it is able to produce lectins that may be involved in the host-pathogen interaction. We focused on the lectin AFL, which was prepared in recombinant form and characterized. Its binding properties were studied using hemagglutination and glycan array analysis. We determined the specificity of the lectin towards l-fucose and fucosylated oligosaccharides, including α1-6 linked core-fucose, which is an important marker for cancerogenesis. Other biologically relevant saccharides such as sialic acid, d-mannose or d-galactose were not bound. Blood group epitopes of the ABH and Lewis systems were recognized, Le(Y) being the preferred ligand among others. To provide a correlation between the observed functional characteristics and structural basis, AFL was crystallized in a complex with methyl-α,L-selenofucoside and its structure was solved using the SAD method. Six binding sites, each with different compositions, were identified per monomer and significant differences from the homologous AAL lectin were found. Structure-derived peptides were utilized to prepare anti-AFL polyclonal antibodies, which suggested the presence of AFL on the Aspergillus' conidia, confirming its expression in vivo. Stimulation of human bronchial cells by AFL led to IL-8 production in a dose-dependent manner. AFL thus probably contributes to the inflammatory response observed upon the exposure of a patient to A. fumigatus. The combination of affinity to human epithelial epitopes, production by conidia and pro-inflammatory activity is remarkable and shows that AFL might be an important virulence factor involved in an early stage of A. fumigatus infection.


  • Organizational Affiliation

    Central European Institute for Technology, Masaryk University, Brno, Czech Republic ; National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, Czech Republic.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FUCOSE-SPECIFIC LECTIN FLEA
A, B, C, D
315Aspergillus fumigatusMutation(s): 1 
UniProt
Find proteins for Q4WW81 (Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293))
Explore Q4WW81 
Go to UniProtKB:  Q4WW81
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ4WW81
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SFU
Query on SFU

Download Ideal Coordinates CCD File 
AA [auth D]
BA [auth D]
CA [auth D]
DA [auth D]
E [auth A]
methyl 1-seleno-alpha-L-fucopyranoside
C7 H14 O4 Se
VHTNTJQSKJZERS-XUVCUMPTSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
CSD
Query on CSD
A, B, C, D
L-PEPTIDE LINKINGC3 H7 N O4 SCYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.60 Å
  • R-Value Free: 0.185 
  • R-Value Work: 0.152 
  • R-Value Observed: 0.154 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.691α = 91.09
b = 79.847β = 88.89
c = 84.389γ = 103
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
HKL2Mapphasing

Structure Validation

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Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted SFUClick on this verticalbar to view details

Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-02-06
    Type: Initial release
  • Version 1.1: 2014-01-08
    Changes: Database references
  • Version 1.2: 2014-11-05
    Changes: Atomic model, Database references, Derived calculations, Non-polymer description, Other, Refinement description, Structure summary
  • Version 1.3: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Derived calculations, Other, Refinement description, Structure summary