2E7P

Crystal structure of the holo form of glutaredoxin C1 from populus tremula x tremuloides

2E7P の概要

• エントリーDOI: 10.2210/pdb2e7p/pdb
• 分子名称: Glutaredoxin, FE2/S2 (INORGANIC) CLUSTER, GLUTATHIONE, ... (4 entities in total)
• 機能のキーワード: thioredoxin fold, glutaredoxin, poplar, electron transport
• 由来する生物種: Populus tremula x Populus tremuloides
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51145.88

構造登録者

Unno, H.,Takahashi, T.,Kawakami, T.,Aimoto, S.,Hase, T.,Kusunoki, M.,Rouhier, N.,Jacquot, J.P. (登録日: 2007-01-12, 公開日: 2007-09-25, 最終更新日: 2024-03-13)

主引用文献

Rouhier, N.,Unno, H.,Bandyopadhyay, S.,Masip, L.,Kim, S.K.,Hirasawa, M.,Gualberto, J.M.,Lattard, V.,Kusunoki, M.,Knaff, D.B.,Georgiou, G.,Hase, T.,Johnson, M.K.,Jacquot, J.P.
Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1
Proc.Natl.Acad.Sci.Usa, 104:7379-7384, 2007

PubMed Abstract: When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron-sulfur-containing holoprotein or as a monomeric apoprotein in solution. Analytical and spectroscopic studies of wild-type protein and site-directed variants and structural characterization of the holoprotein by using x-ray crystallography indicate that the holoprotein contains a subunit-bridging [2Fe-2S] cluster that is ligated by the catalytic cysteines of two glutaredoxins and the cysteines of two glutathiones. Mutagenesis data on a variety of poplar glutaredoxins suggest that the incorporation of an iron-sulfur cluster could be a general feature of plant glutaredoxins possessing a glycine adjacent to the catalytic cysteine. In light of these results, the possible involvement of plant glutaredoxins in oxidative stress sensing or iron-sulfur biosynthesis is discussed with respect to their intracellular localization.

PubMed: 17460036
DOI: 10.1073/pnas.0702268104

実験手法

X-RAY DIFFRACTION (2.1 Å)