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6MYX

EM structure of Bacillus subtilis ribonucleotide reductase inhibited double-helical filament of NrdE alpha subunit with dATP

Summary for 6MYX
Entry DOI10.2210/pdb6myx/pdb
Related6MT9 6MV9 6MVE
EMDB information9272 9293
DescriptorRibonucleoside-diphosphate reductase, 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE (2 entities in total)
Functional Keywordsribonucleotide reductase, allostery, nucleotide metabolism, filament, datp, atp, oxidoreductase, protein fibril
Biological sourceBacillus subtilis
Total number of polymer chains4
Total formula weight327095.33
Authors
Thomas, W.C.,Bacik, J.P.,Chen, J.Z.,Ando, N. (deposition date: 2018-11-02, release date: 2019-06-19, Last modification date: 2024-03-13)
Primary citationThomas, W.C.,Brooks 3rd, F.P.,Burnim, A.A.,Bacik, J.P.,Stubbe, J.,Kaelber, J.T.,Chen, J.Z.,Ando, N.
Convergent allostery in ribonucleotide reductase.
Nat Commun, 10:2653-2653, 2019
Cited by
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 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.
PubMed: 31201319
DOI: 10.1038/s41467-019-10568-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6 Å)
Structure validation

226707

數據於2024-10-30公開中

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