Download MendeleyThree-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution.
Reinemer, P., Dirr, H.W., Ladenstein, R., Huber, R., Lo Bello, M., Federici, G., Parker, M.W.(1992) J Mol Biol 227: 214-226
- PubMed: 1522586
- DOI: https://doi.org/10.1016/0022-2836(92)90692-d
- Primary Citation of Related Structures:
1GSS - PubMed Abstract:
The three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is analyzed and the locations of the binding regions for glutathione (G-site) and electrophilic substrates (H-site) are determined. The specific interactions between protein and the inhibitor's glutathione peptide are the same as those observed between glutathione sulfonate and the porcine isozyme. The H-site is located adjacent to the G-site, with the hexyl moiety lying above a segment (residues 8 to 10) connecting strand beta 1 and helix alpha A where it is in hydrophobic contact with Tyr7, Phe8, Val10, Val35 and Tyr106. Catalytic models are discussed on the basis of the molecular structure.
Organizational Affiliation:
Max-Planck-Institut f¨¹r Biochemie, Martinsried, Germany.
