6W4X

Holocomplex of E. coli class Ia ribonucleotide reductase with GDP and TTP

Summary for 6W4X

• Entry DOI: 10.2210/pdb6w4x/pdb
• EMDB information: 21540
• Descriptor: Ribonucleoside-diphosphate reductase 1 subunit alpha, Ribonucleoside-diphosphate reductase 1 subunit beta, THYMIDINE-5'-TRIPHOSPHATE, ... (7 entities in total)
• Functional Keywords: complex, oxidoreductase
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 4
• Total formula weight: 260687.77

Authors

Kang, G.,Taguchi, A.,Stubbe, J.,Drennan, C.L. (deposition date: 2020-03-11, release date: 2020-04-08, Last modification date: 2024-09-25)

Primary citation

Kang, G.,Taguchi, A.T.,Stubbe, J.,Drennan, C.L.
Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex.
Science, 368:424-427, 2020

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 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.

PubMed: 32217749
DOI: 10.1126/science.aba6794

Experimental method

ELECTRON MICROSCOPY (3.6 Å)