1K3L

Crystal Structure Analysis of S-hexyl-glutathione Complex of Glutathione Transferase at 1.5 Angstroms Resolution

1K3L の概要

• エントリーDOI: 10.2210/pdb1k3l/pdb
• 関連するPDBエントリー: 1K3O 1K3Y
• 分子名称: GLUTATHIONE S-TRANSFERASE A1, S-HEXYLGLUTATHIONE (3 entities in total)
• 機能のキーワード: glutathione s-transferase, s-hexyl glutathione, water structure, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P08263
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51862.83

構造登録者

Le Trong, I.,Stenkamp, R.E.,Ibarra, C.,Atkins, W.M.,Adman, E.T. (登録日: 2001-10-03, 公開日: 2002-10-23, 最終更新日: 2023-08-16)

主引用文献

Le Trong, I.,Stenkamp, R.E.,Ibarra, C.,Atkins, W.M.,Adman, E.T.
1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site
Proteins, 48:618-627, 2002

PubMed Abstract: Cytosolic glutathione S-transferases (GSTs) play a critical role in xenobiotic binding and metabolism, as well as in modulation of oxidative stress. Here, the high-resolution X-ray crystal structures of homodimeric human GSTA1-1 in the apo form and in complex with S-hexyl glutathione (two data sets) are reported at 1.8, 1.5, and 1.3A respectively. At this level of resolution, distinct conformations of the alkyl chain of S-hexyl glutathione are observed, reflecting the nonspecific nature of the hydrophobic substrate binding site (H-site). Also, an extensive network of ordered water, including 75 discrete solvent molecules, traverses the open subunit-subunit interface and connects the glutathione binding sites in each subunit. In the highest-resolution structure, three glycerol moieties lie within this network and directly connect the amino termini of the glutathione molecules. A search for ligand binding sites with the docking program Molecular Operating Environment identified the ordered water network binding site, lined mainly with hydrophobic residues, suggesting an extended ligand binding surface for nonsubstrate ligands, the so-called ligandin site. Finally, detailed comparison of the structures reported here with previously published X-ray structures reveal a possible reaction coordinate for ligand-dependent conformational changes in the active site and the C-terminus.

PubMed: 12211029
DOI: 10.1002/prot.10162

実験手法

X-RAY DIFFRACTION (1.5 Å)