5KQA

Crystal structure of buckwheat glutaredoxin-glutathione complex

5KQA の概要

• エントリーDOI: 10.2210/pdb5kqa/pdb
• 分子名称: Glutaredoxin-glutathione complex, GLUTATHIONE (3 entities in total)
• 機能のキーワード: glutaredoxin, glutathione, complex, monomer, oxidoreductase
• 由来する生物種: Polygonaceae (buckwheat family)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14454.41

構造登録者

Zhang, X.,Wang, W.,Zhao, Y.,Wang, Z.,Wang, H. (登録日: 2016-07-06, 公開日: 2017-07-05, 最終更新日: 2023-11-08)

主引用文献

Zhang, X.,Wang, W.,Li, C.,Zhao, Y.,Yuan, H.,Tan, X.,Wu, L.,Wang, Z.,Wang, H.
Structural insights into the binding of buckwheat glutaredoxin with GSH and regulation of its catalytic activity
J. Inorg. Biochem., 173:21-27, 2017

PubMed Abstract: Glutaredoxins (Grxs) are ubiquitous thioltransferases and members of the thioredoxin (Trx) fold superfamily. They have multiple functions in cells including oxidative stress responses and cell signaling. A novel glutaredoxin from buckwheat (rbGrx) with higher catalytic activity was identified, cloned, and purified. The structures of glutathionylated rbGrx and an rbGrx mutant, in which cysteine 39 was mutated to alanine, were solved by x-ray diffraction at a resolution of 2.05Å and 2.29Å, respectively. In rbGrx, GSH (glutathione) is bound at the conserved GSH-binding site, and its structure shows that it has the potential to function as a scaffold protein for the assembly and delivery of GSH. The crystal structure shows that GSH does not bind to the C39A rbGrx mutant, and the C39A mutant had no catalytic activity, indicating that C39 is a key residue that is involved in both the binding of rbGrx to GSH and the regulation of its catalytic activity. The model showing the binding of GSH with rbGrx provides a basis for understanding its molecular function and its potential future applications in medicinal food science.

PubMed: 28478310
DOI: 10.1016/j.jinorgbio.2017.04.019

実験手法

X-RAY DIFFRACTION (2.05 Å)