+Search query
-Structure paper
Title | Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex. |
---|---|
Journal, issue, pages | Science, Vol. 368, Issue 6489, Page 424-427, Year 2020 |
Publish date | Apr 24, 2020 |
Authors | Gyunghoon Kang / Alexander T Taguchi / JoAnne Stubbe / Catherine L Drennan / |
PubMed Abstract | Ribonucleotide reductases (RNRs) are a diverse family of enzymes that are alone capable of generating 2'-deoxynucleotides de novo and are thus critical in DNA biosynthesis and repair. The nucleotide ...Ribonucleotide reductases (RNRs) are a diverse family of enzymes that are alone capable of generating 2'-deoxynucleotides de novo and are thus critical in DNA biosynthesis and repair. The nucleotide reduction reaction in all RNRs requires the generation of a transient active site thiyl radical, and in class I RNRs, this process involves a long-range radical transfer between two subunits, α and β. Because of the transient subunit association, an atomic resolution structure of an active α2β2 RNR complex has been elusive. We used a doubly substituted β2, E52Q/(2,3,5)-trifluorotyrosine122-β2, to trap wild-type α2 in a long-lived α2β2 complex. We report the structure of this complex by means of cryo-electron microscopy to 3.6-angstrom resolution, allowing for structural visualization of a 32-angstrom-long radical transfer pathway that affords RNR activity. |
External links | Science / PubMed:32217749 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.6 Å |
Structure data | EMDB-21540, PDB-6w4x: |
Chemicals | ChemComp-TTP: ChemComp-MG: ChemComp-GDP: ChemComp-FEO: ChemComp-HOH: |
Source |
|
Keywords | OXIDOREDUCTASE / complex |