3DYR: Crystal Structure Of E. Coli Thioredoxin Mutant I76t In Its Oxidized Form

The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins.
PDB ID: 3DYRDownload
MMDB ID: 69304
PDB Deposition Date: 2008/7/28
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 3DYR: monomeric; determined by software (PISA)
Molecular Components in 3DYR
Label Count Molecule
Protein (1 molecule)
Thioredoxin-1(Gene symbol: trxA)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB