Convergent allostery in ribonucleotide reductase

William C. Thomas, F. Phil Brooks, Audrey A. Burnim, John-Paul Bacik, JoAnne Stubbe, Jason T. Kaelber, James Z. Chen and Nozomi Ando ()
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William C. Thomas: Cornell University
F. Phil Brooks: Princeton University
Audrey A. Burnim: Cornell University
John-Paul Bacik: Cornell University
JoAnne Stubbe: Massachusetts Institute of Technology
Jason T. Kaelber: Rutgers University
James Z. Chen: Oregon Health & Science University
Nozomi Ando: Cornell University

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-10568-4

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