4TR0

Crystal structure of GSSG-bound cGrx2

4TR0 の概要

• エントリーDOI: 10.2210/pdb4tr0/pdb
• 関連するPDBエントリー: 4TR1
• 分子名称: Glutaredoxin 3, ACETATE ION, OXIDIZED GLUTATHIONE DISULFIDE, ... (4 entities in total)
• 機能のキーワード: glutaredoxin, gssg, oxidoreductase
• 由来する生物種: Alkaliphilus oremlandii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22663.63

構造登録者

Lee, E.H.,Hwang, K.Y. (登録日: 2014-06-13, 公開日: 2014-10-01, 最終更新日: 2024-11-13)

主引用文献

Lee, E.H.,Kim, H.Y.,Hwang, K.Y.
The GSH- and GSSG-bound structures of glutaredoxin from Clostridium oremlandii.
Arch.Biochem.Biophys., 564C:20-25, 2014

PubMed Abstract: Glutaredoxin (Grx) is a major redox enzyme that reduces disulfide bonds using glutathione (GSH) as an electron donor. The anaerobic bacterium Clostridium oremlandii possesses a selenocysteine-containing Grx (cGrx1) and a cysteine-containing homolog (cGrx2). Here, the crystal structure of the GSSG-bound form of cGrx2 was determined for the first time at a resolution of 1.95Å. In addition, its monothiol variant cGrx2/C15S in complex with GSH was also determined at a resolution of 1.58Å. cGrx2 is a monomeric protein with an overall structure that consists of the typical thioredoxin fold composed of four α-helices and four β-strands. Two ligands, GSH and GSSG, share a conserved binding site consisting of CPYC, TVP, and CDD motifs. The cysteinyl and γ-glutamyl moieties show similar binding interactions in the two structures, whereas the glycine moiety shows different interactions. Interestingly, the structures revealed that only one GSH moiety of GSSG is sufficient for its binding to the protein. The GSSG-bound structure of cGrx2 was obtained as an oxidized form with a disulfide bond at the CPYC motif. Comparison of the GSH-binding mode in cGrx2 to other known Grxs revealed similarities as well as some diversity.

PubMed: 25218089
DOI: 10.1016/j.abb.2014.09.001

実験手法

X-RAY DIFFRACTION (1.951 Å)