Ribonucleotide reductase: Difference between revisions

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<StructureSection load='1xjg' size='350' side='right' caption='Class II ribonucleotide reductase dimer complex with dATP, UDP (stick models) and Mg+2 ion (green) (PDB entry [[1xjg]])' scene=''>
<StructureSection load='1xjg' size='450' side='right' caption='Class II ribonucleotide reductase dimer complex with dATP, UDP (stick models) and Mg+2 ion (green) (PDB entry [[1xjg]])' scene='46/461381/Cv/1'>
== Function ==
== Function ==
'''Ribonucleotide reductase''' (RNR) catalyzes the formation of deoxyribonucleotides from ribonucleotides<ref>PMID:16756507</ref>.  There are 3 classes of RNR.<br />
'''Ribonucleotide reductase''' (RNR) catalyzes the formation of deoxyribonucleotides from ribonucleotides<ref>PMID:16756507</ref>.  There are 3 classes of RNR.<br />

Revision as of 12:28, 11 August 2016

Function

Ribonucleotide reductase (RNR) catalyzes the formation of deoxyribonucleotides from ribonucleotides[1]. There are 3 classes of RNR.

  • Class I 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 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.

Relevance

RNR inhibitors are studied as therapeutic antiviral, antibacterial and anti-cancer drugs[2].

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 [3]

Class II ribonucleotide reductase dimer complex with dATP, UDP (stick models) and Mg+2 ion (green) (PDB entry 1xjg)

Drag the structure with the mouse to rotate

3D Structures of Ribonucleotide reductase3D Structures of Ribonucleotide reductase

Updated on 11-August-2016

ReferencesReferences

  1. Nordlund P, Reichard P. Ribonucleotide reductases. Annu Rev Biochem. 2006;75:681-706. PMID:16756507 doi:http://dx.doi.org/10.1146/annurev.biochem.75.103004.142443
  2. Munro JB, Silva JC. Ribonucleotide reductase as a target to control apicomplexan diseases. Curr Issues Mol Biol. 2012;14(1):9-26. Epub 2011 Jul 26. PMID:21791713
  3. Larsson KM, Jordan A, Eliasson R, Reichard P, Logan DT, Nordlund P. Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase. Nat Struct Mol Biol. 2004 Nov;11(11):1142-9. Epub 2004 Oct 10. PMID:15475969 doi:http://dx.doi.org/10.1038/nsmb838

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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