4ASL

Structure of Epa1A in complex with the T-antigen (Gal-b1-3- GalNAc)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.24 Å
  • R-Value Free: 0.155 
  • R-Value Work: 0.117 
  • R-Value Observed: 0.119 

wwPDB Validation   3D Report Full Report


This is version 3.0 of the entry. See complete history


Literature

Structural Basis for Promiscuity and Specificity During Candida Glabrata Invasion of Host Epithelia.

Maestre-Reyna, M.Diderrich, R.Veelders, M.S.Eulenburg, G.Kalugin, V.Bruckner, S.Keller, P.Rupp, S.Mosch, H.Essen, L.-O.

(2012) Proc Natl Acad Sci U S A 109: 16864

  • DOI: https://doi.org/10.1073/pnas.1207653109
  • Primary Citation of Related Structures:  
    4AF9, 4AFA, 4AFB, 4AFC, 4ASL

  • PubMed Abstract: 

    The human pathogenic yeast Candida glabrata harbors more than 20 surface-exposed, epithelial adhesins (Epas) for host cell adhesion. The Epa family recognizes host glycans and discriminates between target tissues by their adhesin (A) domains, but a detailed structural basis for ligand-binding specificity of Epa proteins has been lacking so far. In this study, we provide high-resolution crystal structures of the Epa1A domain in complex with different carbohydrate ligands that reveal how host cell mucin-type O-glycans are recognized and allow a structure-guided classification of the Epa family into specific subtypes. Further detailed structural and functional characterization of subtype-switched Epa1 variants shows that specificity is governed by two inner loops, CBL1 and CBL2, involved in calcium binding as well as by three outer loops, L1, L2, and L3. In summary, our study provides the structural basis for promiscuity and specificity of Epa adhesins, which might further contribute to developing anti-adhesive antimycotics and combating Candida colonization.


  • Organizational Affiliation

    Biomedical Research Center/Department of Chemistry, Philipps-Universität Marburg, D-35032 Marburg, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
EPA1P259Nakaseomyces glabratusMutation(s): 0 
UniProt
Find proteins for Q6FUW5 (Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138))
Explore Q6FUW5 
Go to UniProtKB:  Q6FUW5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6FUW5
Sequence Annotations
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  • Reference Sequence
Oligosaccharides

Help

Entity ID: 2
MoleculeChains Length2D Diagram Glycosylation3D Interactions
beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose
B
2N/A
Glycosylation Resources
GlyTouCan:  G01534TU
GlyCosmos:  G01534TU
GlyGen:  G01534TU
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.24 Å
  • R-Value Free: 0.155 
  • R-Value Work: 0.117 
  • R-Value Observed: 0.119 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 74.6α = 89.9
b = 103.9β = 90
c = 69.4γ = 89.9
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
SCALAdata scaling
XSCALEdata scaling
REFMACphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-10-17
    Type: Initial release
  • Version 1.1: 2012-11-07
    Changes: Database references
  • Version 2.0: 2017-06-14
    Changes: Advisory, Atomic model, Derived calculations
  • Version 3.0: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Advisory, Atomic model, Data collection, Derived calculations, Other, Structure summary