CATH Classification

Domain Context

CATH Clusters

Superfamily 3.20.70.20
Functional Family

Enzyme Information

1.1.98.6
Ribonucleoside-triphosphate reductase (formate).
based on mapping to UniProt P07071
Ribonucleoside 5'-triphosphate + formate = 2'-deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O.
-!- The enzyme, which is expressed in the bacterium Escherichia coli during anaerobic growth, contains an iron sulfur center. -!- The active form of the enzyme contains an oxygen-sensitive glycyl (1-amino-2-oxoethan-1-yl) radical that is generated by the activating enzyme NrdG via chemistry involving S-adenosylmethionine (SAM) and a [4Fe-4S] cluster. -!- The glycyl radical is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. -!- The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl (1-lambda(4)-disulfan-1-yl) radical bridge between methionine and cysteine residues. -!- Oxidation of formate by the thiosulfuranyl radical results in the release of CO(2) and regeneration of the thiyl radical. -!- Cf. EC 1.17.4.1 and EC 1.17.4.2.

UniProtKB Entries (1)

P07071
NRDD_BPT4
Escherichia virus T4
Anaerobic ribonucleoside-triphosphate reductase

PDB Structure

PDB 1H7A
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Basis for Allosteric Substrate Specificty Regulation in Anaerobic Ribonucleotide Reductase
Larsson, K.-M., Andersson, J., Sjoeberg, B.-M., Nordlund, P., Logan, D.T.
Structure