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Convergent allostery in ribonucleotide reductase

Author

Listed:
  • William C. Thomas

    (Cornell University
    Princeton University)

  • F. Phil Brooks

    (Princeton University)

  • Audrey A. Burnim

    (Cornell University
    Princeton University)

  • John-Paul Bacik

    (Cornell University
    Princeton University)

  • JoAnne Stubbe

    (Massachusetts Institute of Technology)

  • Jason T. Kaelber

    (Rutgers University)

  • James Z. Chen

    (Oregon Health & Science University)

  • Nozomi Ando

    (Cornell University
    Princeton University)

Abstract

Ribonucleotide reductases (RNRs) use a conserved radical-based mechanism to catalyze the conversion of ribonucleotides to deoxyribonucleotides. Within the RNR family, class Ib RNRs are notable for being largely restricted to bacteria, including many pathogens, and for lacking an evolutionarily mobile ATP-cone domain that allosterically controls overall activity. In this study, we report the emergence of a distinct and unexpected mechanism of activity regulation in the sole RNR of the model organism Bacillus subtilis. Using a hypothesis-driven structural approach that combines the strengths of small-angle X-ray scattering (SAXS), crystallography, and cryo-electron microscopy (cryo-EM), we describe the reversible interconversion of six unique structures, including a flexible active tetramer and two inhibited helical filaments. These structures reveal the conformational gymnastics necessary for RNR activity and the molecular basis for its control via an evolutionarily convergent form of allostery.

Suggested Citation

  • William C. Thomas & F. Phil Brooks & Audrey A. Burnim & John-Paul Bacik & JoAnne Stubbe & Jason T. Kaelber & James Z. Chen & Nozomi Ando, 2019. "Convergent allostery in ribonucleotide reductase," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10568-4
    DOI: 10.1038/s41467-019-10568-4
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