1vdc
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STRUCTURE OF NADPH DEPENDENT THIOREDOXIN REDUCTASE
OverviewOverview
Thioredoxin exists in all organisms and is responsible for the hydrogen, transfer to important enzymes for ribonucleotide reduction and the, reduction of methionine sulphoxide and sulphate. Thioredoxins have also, been shown to regulate enzyme activity in plants and are also involved in, the regulation of transcription factors and several other regulatory, activities. Thioredoxin is reduced by the flavoenzyme thioredoxin, reductase using NADPH. We have now determined the first structure of a, eukaryotic thioredoxin reductase, from the plant Arabidopsis thaliana, at, 2.5 A resolution. The dimeric A. thaliana thioredoxin reductase is, structurally similar to that of the Escherichia coli enzyme, and most, differences occur in the loops. Because the plant and E. coli enzymes have, the same ... [(full description)]
About this StructureAbout this Structure
1VDC is a [Single protein] structure of sequence from [Arabidopsis thaliana] with SO4 and FAD as [ligands]. Active as [Transferred entry: 1.8.1.9], with EC number [1.6.4.5]. Structure known Active Sites: ACT and FAD. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution., Dai S, Saarinen M, Ramaswamy S, Meyer Y, Jacquot JP, Eklund H, J Mol Biol. 1996 Dec 20;264(5):1044-57. PMID:9000629
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