1GLP

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

1GLP の概要

• エントリーDOI: 10.2210/pdb1glp/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE YFYF, GLUTATHIONE SULFONIC ACID (3 entities in total)
• 機能のキーワード: transferase(glutathione)
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm : P19157
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47718.57

構造登録者

Garcia-Saez, I.,Coll, M. (登録日: 1994-03-07, 公開日: 1994-06-22, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)