Ribonucleotide reductase

spinqualitylabelsall models Class II ribonucleotide reductase dimer complex with dATP, UDP and Mg+2 ion (green) (PDB entry 1xjg) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Ribonucleotide reductase (RNR) or ribonucleotide-diphosphate reductase catalyzes the formation of deoxyribonucleotides from ribonucleotides. There are 3 classes of RNR. Class Ia RNR is a tetramer composed from large (RNR1) and small (RNR2) subunits. Class I RNR is iron-dependent and produces tyrosyl radical. Thimidine triphosphate (TTP) is an effector in the reaction. Class Ib RNR contains 2 proteins: α (NrdE) and β (NrdF). E. Coli contains two types of RNR: the aerobic RNR belongs to class Ia and is composed of proteins R1 and R2, the anaerobic RNR belongs to class Ib. Class II RNR reduces ribonucleotide triphosphates using coenzyme B12. Class III RNR generate glycine radical using S-adenosyl methionine and Fe-S center. For details on human RNR2 see P53R2. For mouse RNR see Mouse Ribonucleotide Reductase R2. For RNR small subunit with nitrotyrosine modification see Nitrotyrosine. See also Ribonucleotide Reductase. Relevance RNR inhibitors are studied as therapeutic antiviral, antibacterial and anti-cancer drugs. Structural highlights Class II RNR is vitamin B12-dependent. The active site which binds the substrate is in a tight pocket and contains conserved residues involved in the catalytic mechanism . dATP binding site. Water molecules are shown as red spheres. UDP binding site. 3D Structures of Ribonucleotide reductase Ribonucleotide reductase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman