1T00
The structure of thioredoxin from S. coelicolor
Summary for 1T00
| Entry DOI | 10.2210/pdb1t00/pdb |
| Descriptor | Thioredoxin (2 entities in total) |
| Functional Keywords | thioredoxin, s. coelicolor, redox regulation, multifunction macromolecule, electron transport |
| Biological source | Streptomyces coelicolor |
| Total number of polymer chains | 1 |
| Total formula weight | 12128.78 |
| Authors | Stefankova, P. (deposition date: 2004-04-07, release date: 2005-01-25, Last modification date: 2024-02-14) |
| Primary citation | 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 Cited by 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: 16510983DOI: 10.1107/S1744309104032993 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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