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Structure paper

TitleStructure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex.
Journal, issue, pagesScience, Vol. 368, Issue 6489, Page 424-427, Year 2020
Publish dateApr 24, 2020
AuthorsGyunghoon Kang / Alexander T Taguchi / JoAnne Stubbe / Catherine L Drennan /
PubMed AbstractRibonucleotide 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 linksScience / PubMed:32217749 / PubMed Central
MethodsEM (single particle)
Resolution3.6 Å
Structure data

21540

6w4x

EMDB-21540, PDB-6w4x:
Holocomplex of E. coli class Ia ribonucleotide reductase with GDP and TTP
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-TTP:
THYMIDINE-5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-FEO:
MU-OXO-DIIRON

ChemComp-HOH:
WATER

Source
  • Escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
KeywordsOXIDOREDUCTASE / complex

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