CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.20 | Alpha-Beta Barrel | |
3.20.70 | Anaerobic Ribonucleotide-triphosphate Reductase Large Chain | |
3.20.70.20 |
Domain Context
CATH Clusters
Superfamily | 3.20.70.20 |
Functional Family | Anaerobic ribonucleoside-triphosphate reductase, NrdD |
Enzyme Information
1.17.4.2 |
Ribonucleoside-triphosphate reductase (thioredoxin).
based on mapping to UniProt P07071
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O = ribonucleoside triphosphate + thioredoxin.
-!- The enzyme, characterized from the bacterium Lactobacillus leichmannii, is similar to class II ribonucleoside-diphosphate reductase (cf. EC 1.17.4.1); however, it is specific for the triphosphate versions of its substrates. -!- The enzyme contains an adenosylcobalamin cofactor that is involved in generation of a transient thiyl radical on a cysteine residue. -!- This radical attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6.
|
UniProtKB Entries (1)
P07071 |
NRDD_BPT4
Enterobacteria phage T4
Anaerobic ribonucleoside-triphosphate reductase
|
PDB Structure
PDB | 1H78 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural Basis for Allosteric Substrate Specificty Regulation in Anaerobic Ribonucleotide Reductase
Structure
|