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1t00
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(New page: 200px<br /><applet load="1t00" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t00, resolution 1.51Å" /> '''The structure of thi...)
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Revision as of 00:45, 21 November 2007
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The structure of thioredoxin from S. coelicolor
Overview
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.
About this Structure
1T00 is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.
Reference
Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor., Stefankova P, Maderova J, Barak I, Kollarova M, Otwinowski Z, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Feb 1;61(Pt, 2):164-8. Epub 2005 Jan 8. PMID:16510983
Page seeded by OCA on Wed Nov 21 02:53:09 2007
