Cloned (Comment) | Organism |
---|---|
- |
Mus musculus |
Crystallization (Comment) | Organism |
---|---|
structure of the catalytic domain of mouse deiodinase Dio3, to 1.9 A resolution. The catalytic Sec170 is positioned in the loop connecting beta1 to alpha1. It points toward an elongated cleft that likely represents the iodothyronine binding site. The deiodination step follows a selenolate inline attack on the iodine delta-hole weakening the carbon-iodine bond. The abstracted iodonium is replaced by a proton approaching from the opposite side of the ring. The proton is conveyed to the 5-position of the iodothyronine along a triad His219, Glu200, and Ser167, with residues Tyr197 and Thr169 participating in the organization of an intricate H-bond network | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
E200T | inactive | Mus musculus |
S167A | about 10% residual activity | Mus musculus |
Sec170C | mutation in active site, crystallization data | Mus musculus |
T169A | inactive | Mus musculus |
T169S | 60% of wild-type activity | Mus musculus |
Y197F | inactive | Mus musculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
37000 | - |
2 * 37000, epitope-tagged recombinant protein,SDS-PAGE | Mus musculus |
50000 | 55000 | FLAG-tagged recombinant protein, PAGE | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q91ZI8 | - |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 37000, epitope-tagged recombinant protein,SDS-PAGE | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
Dio3 | - |
Mus musculus |