1M9A

Crystal structure of the 26 kDa glutathione S-transferase from Schistosoma japonicum complexed with S-hexylglutathione

1M9A の概要

• エントリーDOI: 10.2210/pdb1m9a/pdb
• 関連するPDBエントリー: 1GNE 1GTA 1GTB 1M99 1M9B
• 分子名称: Glutathione S-Transferase 26 kDa, S-HEXYLGLUTATHIONE (3 entities in total)
• 機能のキーワード: glutathione transferase, antigen, multigene family, transferase
• 由来する生物種: Schistosoma japonicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25927.21

構造登録者

Cardoso, R.M.F.,Daniels, D.S.,Bruns, C.M.,Tainer, J.A. (登録日: 2002-07-28, 公開日: 2003-03-04, 最終更新日: 2024-02-14)

主引用文献

Cardoso, R.M.F.,Daniels, D.S.,Bruns, C.M.,Tainer, J.A.
Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum
PROTEINS: STRUCT.,FUNCT.,GENET., 51:137-146, 2003

PubMed Abstract: The 26-kDa glutathione S-transferase from Schistosoma japonicum (Sj26GST), a helminth worm that causes schistosomiasis, catalyzes the conjugation of glutathione with toxic secondary products of membrane lipid peroxidation. Crystal structures of Sj26GST in complex with glutathione sulfonate (Sj26GSTSLF), S-hexyl glutathione (Sj26GSTHEX), and S-2-iodobenzyl glutathione (Sj26GSTIBZ) allow characterization of the electrophile binding site (H site) of Sj26GST. The S-hexyl and S-2-iodobenzyl moieties of these product analogs bind in a pocket defined by side-chains from the beta1-alpha1 loop (Tyr7, Trp8, Ile10, Gly12, Leu13), helix alpha4 (Arg103, Tyr104, Ser107, Tyr111), and the C-terminal coil (Gln204, Gly205, Trp206, Gln207). Changes in the Ser107 and Gln204 dihedral angles make the H site more hydrophobic in the Sj26GSTHEX complex relative to the ligand-free structure. These structures, together with docking studies, indicate a possible binding mode of Sj26GST to its physiologic substrates 4-hydroxynon-2-enal (4HNE), trans-non-2-enal (NE), and ethacrynic acid (EA). In this binding mode, hydrogen bonds of Tyr111 and Gln207 to the carbonyl oxygen atoms of 4HNE, NE, and EA could orient the substrates and enhance their electrophilicity to promote conjugation with glutathione.

PubMed: 12596270
DOI: 10.1002/prot.10345

実験手法

X-RAY DIFFRACTION (2.1 Å)