Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Petra StefankovaZbyszek Otwinowski

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.

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Citations

Nov 6, 2013·Acta Crystallographica. Section D, Biological Crystallography·Jaclyn BibbyDaniel J Rigden
Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Karen Fulan DiscolaBeatriz Gomes Guimarães

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