1GSS

THREE-DIMENSIONAL STRUCTURE OF CLASS PI GLUTATHIONE S-TRANSFERASE FROM HUMAN PLACENTA IN COMPLEX WITH S-HEXYLGLUTATHIONE AT 2.8 ANGSTROMS RESOLUTION

Summary for 1GSS

• Entry DOI: 10.2210/pdb1gss/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, L-gamma-glutamyl-S-hexyl-L-cysteinylglycine (3 entities in total)
• Functional Keywords: glutathione, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 47276.11

Authors

Reinemer, P.,Dirr, H.W.,Ladenstein, R.,Lobello, M.,Federici, G.,Huber, R.,Parker, M.W. (deposition date: 1992-05-28, release date: 1994-01-31, Last modification date: 2024-02-07)

Primary citation

Reinemer, P.,Dirr, H.W.,Ladenstein, R.,Huber, R.,Lo Bello, M.,Federici, G.,Parker, M.W.
Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution.
J.Mol.Biol., 227:214-226, 1992

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.

PubMed: 1522586
DOI: 10.1016/0022-2836(92)90692-D

Experimental method

X-RAY DIFFRACTION (2.8 Å)