1T00

The structure of thioredoxin from S. coelicolor

1T00 の概要

• エントリーDOI: 10.2210/pdb1t00/pdb
• 分子名称: Thioredoxin (2 entities in total)
• 機能のキーワード: thioredoxin, s. coelicolor, redox regulation, multifunction macromolecule, electron transport
• 由来する生物種: Streptomyces coelicolor
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12128.78

構造登録者

Stefankova, P. (登録日: 2004-04-07, 公開日: 2005-01-25, 最終更新日: 2024-02-14)

主引用文献

Stefankova, P.,Maderova, J.,Barak, I.,Kollarova, M.,Otwinowski, Z.
Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor.
Acta Crystallogr.,Sect.F, 61:164-168, 2005

PubMed Abstract: Thioredoxins are ubiquitous proteins that serve as reducing agents and general protein disulfide reductases. In turn, they are reduced by electrons obtained from the NADPH-containing thioredoxin reductase. Thioredoxins have been isolated and characterized from a large number of organisms. The Gram-positive bacterium Streptomyces coelicolor contains three thioredoxins that are involved in unknown biological processes. trxA from S. coelicolor was cloned and expressed in Escherichia coli and the protein purified and crystallized using the hanging-drop method of vapour diffusion. The crystal structure of thioredoxin A has been determined at 1.5 A resolution using a synchrotron-radiation source. The protein reveals a thioredoxin-like fold with a typical CXXC active site. The crystal exhibits the symmetry of space group P2(1)2(1)2, with unit-cell parameters a = 43.6, b = 71.8, c = 33.2 A.

PubMed: 16510983
DOI: 10.1107/S1744309104032993

実験手法

X-RAY DIFFRACTION (1.51 Å)