2R6K

Crystal structure of an I71V hGSTA1-1 mutant in complex with S-hexylglutathione


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.51 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.211 

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This is version 1.4 of the entry. See complete history


Literature

The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function.

Achilonu, I.Gildenhuys, S.Fisher, L.Burke, J.Fanucchi, S.Sewell, B.T.Fernandes, M.Dirr, H.W.

(2010) Acta Crystallogr Sect F Struct Biol Cryst Commun 66: 776-780

  • DOI: https://doi.org/10.1107/S1744309110019135
  • Primary Citation of Related Structures:  
    2R6K, 3KTL

  • PubMed Abstract: 

    The common fold shared by members of the glutathione-transferase (GST) family has a topologically conserved isoleucine residue at the N-terminus of helix 3 which is involved in the packing of helix 3 against two beta-strands in domain 1. The role of the isoleucine residue in the structure, function and stability of GST was investigated by replacing the Ile71 residue in human GSTA1-1 by alanine or valine. The X-ray structures of the I71A and I71V mutants resolved at 1.75 and 2.51 A, respectively, revealed that the mutations do not alter the overall structure of the protein compared with the wild type. Urea-induced equilibrium unfolding studies using circular dichroism and tryptophan fluorescence suggest that the mutation of Ile71 to alanine or valine reduces the stability of the protein. A functional assay with 1-chloro-2,4-dinitrobenzene shows that the mutation does not significantly alter the function of the protein relative to the wild type. Overall, the results suggest that conservation of the topologically conserved Ile71 maintains the structural stability of the protein but does not play a significant role in catalysis and substrate binding.


  • Organizational Affiliation

    Protein Structure-Function Research Unit, School of Molecular and Cell Biology, University of the Witwatersrand, Johannesburg 2050, South Africa.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glutathione S-transferase A1
A, B
222Homo sapiensMutation(s): 1 
Gene Names: GSTA1
EC: 2.5.1.18
UniProt & NIH Common Fund Data Resources
Find proteins for P08263 (Homo sapiens)
Explore P08263 
Go to UniProtKB:  P08263
PHAROS:  P08263
GTEx:  ENSG00000243955 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08263
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.51 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.206 
  • R-Value Observed: 0.211 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 98.409α = 90
b = 93.577β = 93.05
c = 50.717γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction
HKL-2000data collection

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-08-19
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Refinement description
  • Version 1.3: 2021-10-20
    Changes: Database references, Derived calculations
  • Version 1.4: 2023-08-30
    Changes: Data collection, Refinement description