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-Structure paper
Title | Convergent allostery in ribonucleotide reductase. |
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Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 2653, Year 2019 |
Publish date | Jun 14, 2019 |
Authors | William C Thomas / F Phil Brooks / Audrey A Burnim / John-Paul Bacik / JoAnne Stubbe / Jason T Kaelber / James Z Chen / Nozomi Ando / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:31201319 / PubMed Central |
Methods | EM (helical sym.) / X-ray diffraction |
Resolution | 2.5 - 6.0 Å |
Structure data | EMDB-9272, PDB-6mw3: EMDB-9293, PDB-6myx: PDB-6mt9: PDB-6mv9: PDB-6mve: |
Chemicals | ChemComp-TTP: ChemComp-ADP: ChemComp-ATP: ChemComp-MG: ChemComp-HOH: ChemComp-DTP: |
Source |
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Keywords | OXIDOREDUCTASE / ribonucleotide reductase / allostery / nucleotide metabolism / dATP / ATP / filament / PROTEIN FIBRIL |