2GSQ

GLUTATHIONE S-TRANSFERASE FROM SQUID DIGESTIVE GLAND COMPLEXED WITH S-(3-IODOBENZYL)GLUTATHIONE

2GSQ の概要

• エントリーDOI: 10.2210/pdb2gsq/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE, SULFATE ION, S-(3-IODOBENZYL)GLUTATHIONE, ... (4 entities in total)
• 機能のキーワード: squid digestive gland, sigma class, transferase
• 由来する生物種: Ommastrephes sloani (Sloane's squid)
• 細胞内の位置: Cytoplasm: P46088
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23963.33

構造登録者

Ji, X.,Armstrong, R.N.,Gilliland, G.L. (登録日: 1995-04-14, 公開日: 1996-04-12, 最終更新日: 2023-08-30)

主引用文献

Ji, X.,von Rosenvinge, E.C.,Johnson, W.W.,Armstrong, R.N.,Gilliland, G.L.
Location of a potential transport binding site in a sigma class glutathione transferase by x-ray crystallography.
Proc.Natl.Acad.Sci.USA, 93:8208-8213, 1996

PubMed Abstract: The crystal structure of the sigma class glutathione transferase from squid digestive gland in complex with S-(3-iodobenzyl)glutathione reveals a third binding site for the glutathione conjugate besides the two in the active sites of the dimer. The additional binding site is near the crystallographic two-fold axis between the two alpha 4-turn-alpha 5 motifs. The principal binding interactions with the conjugate include specific electrostatic interactions between the peptide and the two subunits and a hydrophobic cavity found across the two-fold axis that accommodates the 3-iodobenzyl group. Thus, two identical, symmetry-related but mutually exclusive binding modes for the third conjugate are observed. The hydrophobic pocket is about 14 A from the hydroxyl group of Tyr-7 in the active site. This site is a potential transport binding site for hydrophobic molecules or their glutathione conjugates.

PubMed: 8710848
DOI: 10.1073/pnas.93.16.8208

実験手法

X-RAY DIFFRACTION (2.2 Å)