4LMW

Crystal structure of glutathione transferase GSTFuA3 from Phanerochaete chrysosporium


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.099 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.187 

wwPDB Validation 3D Report Full Report


This is version 1.0 of the entry. See complete history

Literature

Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.

Mathieu, Y.Prosper, P.Favier, F.Harvengt, L.Didierjean, C.Jacquot, J.P.Morel-Rouhier, M.Gelhaye, E.

(2013) Plos One 8: e80298-e80298

  • DOI: 10.1371/journal.pone.0080298
  • Primary Citation of Related Structures:  

  • PubMed Abstract: 
  • Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fung ...

    Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry.


    Organizational Affiliation

    Université de Lorraine, IAM, UMR 1136, IFR 110 EFABA, Vandoeuvre-les-Nancy, France ; INRA, IAM, UMR 1136, Champenoux, France ; Laboratoire de biotechnologie, Pôle Biotechnologie et Sylviculture Avancée, FCBA, Campus Forêt-Bois de Pierroton, Cestas, France.




Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
Glutathione transferase
A
251Phanerochaete chrysosporiumMutation(s): 0 
EC: 2.5.1.18
Find proteins for A0A067XG73 (Phanerochaete chrysosporium)
Go to UniProtKB:  A0A067XG73
Small Molecules
Ligands 1 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
FMT
Query on FMT

Download SDF File 
Download CCD File 
A
FORMIC ACID
C H2 O2
BDAGIHXWWSANSR-UHFFFAOYSA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.099 Å
  • R-Value Free: 0.216 
  • R-Value Work: 0.187 
  • Space Group: P 61 2 2
Unit Cell:
Length (Å)Angle (°)
a = 87.000α = 90.00
b = 87.000β = 90.00
c = 225.703γ = 120.00
Software Package:
Software NamePurpose
XDSdata reduction
Proxima1data collection
PHENIXrefinement
SCALAdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History 

Deposition Data

Revision History 

  • Version 1.0: 2014-05-28
    Type: Initial release