1T00: The Structure Of Thioredoxin From S. Coelicolor

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.
PDB ID: 1T00Download
MMDB ID: 31239
PDB Deposition Date: 2004/4/7
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 1.51  Å
Source Organism:
Similar Structures:
Biological Unit for 1T00: monomeric; determined by author
Molecular Components in 1T00
Label Count Molecule
Protein (1 molecule)
Thioredoxin(Gene symbol: SCO3889)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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