4F0B

Crystal structure of the glutathione transferase URE2P1 from Phanerochaete chrysosporium.

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.165 
  • R-Value Work: 0.141 
  • R-Value Observed: 0.142 

Starting Model: experimental
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This is version 1.2 of the entry. See complete history. 


Literature

Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium.

Thuillier, A., Roret, T., Favier, F., Gelhaye, E., Jacquot, J.P., Didierjean, C., Morel-Rouhier, M.

(2013) FEBS Lett 587: 2125-2130

  • DOI: https://doi.org/10.1016/j.febslet.2013.05.031
  • Primary Citation of Related Structures:  
    4F0B

  • PubMed Abstract: 

    Glutathione transferases (GSTs) are known to transfer glutathione onto small hydrophobic molecules in detoxification reactions. The GST Ure2pB1 from Phanerochaete chrysosporium exhibits atypical features, i.e. the presence of two glutathione binding sites and a high affinity towards oxidized glutathione. Moreover, PcUre2pB1 is able to efficiently deglutathionylate GS-phenacylacetophenone. Catalysis is not mediated by the cysteines of the protein but rather by the one of glutathione and an asparagine residue plays a key role in glutathione stabilization. Interestingly PcUre2pB1 interacts in vitro with a GST of the omega class. These properties are discussed in the physiological context of wood degrading fungi.

    • Organizational Affiliation: 

    Université de Lorraine, IAM, UMR 1136, IFR 110 EFABA,Vandoeuvre-lès-Nancy F-54506, France.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
THIOL TRANSFERASE
A, B
224Phanerodontia chrysosporiumMutation(s): 0 
EC: 2.5.1.18
UniProt
Find proteins for I7A570 (Phanerodontia chrysosporium)
Explore I7A570 
Go to UniProtKB:  I7A570
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupI7A570
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.165 
  • R-Value Work: 0.141 
  • R-Value Observed: 0.142 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.907α = 90
b = 53.947β = 90
c = 165.225γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
MOLREPphasing
PHENIXrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-06-12
    Type: Initial release
  • Version 1.1: 2013-07-17
    Changes: Database references
  • Version 1.2: 2023-09-13
    Changes: Data collection, Database references, Derived calculations, Refinement description