2GLR

MOLECULAR STRUCTURE AT 1.8 ANGSTROMS OF MOUSE LIVER CLASS PI GLUTATHIONE S-TRANSFERASE COMPLEXED WITH S-(P-NITROBENZYL)GLUTATHIONE AND OTHER INHIBITORS

Summary for 2GLR

• Entry DOI: 10.2210/pdb2glr/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE YFYF, S-HEXYLGLUTATHIONE (3 entities in total)
• Functional Keywords: transferase(glutathione)
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm : P19157
• Total number of polymer chains: 2
• Total formula weight: 47792.91

Authors

Parraga, A.,Garcia-Saez, I.,Coll, M. (deposition date: 1994-05-04, release date: 1994-07-31, Last modification date: 2024-02-14)

Primary citation

Garcia-Saez, I.,Parraga, A.,Phillips, M.F.,Mantle, T.J.,Coll, M.
Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors.
J.Mol.Biol., 237:298-314, 1994

PubMed Abstract: The three-dimensional crystal structure of pi class glutathione S-transferase YfYf from mouse liver complexed with the inhibitor S-(p-nitrobenzyl)glutathione has been determined at 1.8 A resolution by X-ray diffraction. In addition two complexes with glutathione sulphonic acid and S-hexylglutathione have been determined at resolutions of 1.9 and 2.2 A, respectively. The high resolution of the S-(p-nitrobenzyl)glutathione complex allows a detailed analysis of the active site including the hydrophobic (H-) subsite. The nitrobenzyl moiety occupies a hydrophobic pocket with its aromatic ring sandwiched between Phe8 and the hydroxyl group of Tyr108. An insertion of two residues Gly41 and Leu42, with respect to the pig enzyme, splits helix alpha B into an alpha-helix and a 3(10) helix. Water bridges between carbonyl oxygen atoms of the alpha-helix at its C terminus and the amide NH groups of the 3(10) helix at its N terminus provide structural continuity between these two secondary elements. Tyr7 appears to be the only residue close to the sulphur atom of glutathione, while three conserved water molecules lie in the surrounding area in all complexes. The enzyme mechanism is discussed on the basis of the structural analysis.

PubMed: 8145243
DOI: 10.1006/jmbi.1994.1232

Experimental method

X-RAY DIFFRACTION (2.2 Å)