Fig. 2: Mechanism of NrdR function involving dodecameric, octameric, and tetrameric structures. | Nature Communications

Fig. 2: Mechanism of NrdR function involving dodecameric, octameric, and tetrameric structures.

From: A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases

Fig. 2: Mechanism of NrdR function involving dodecameric, octameric, and tetrameric structures.The alt text for this image may have been generated using AI.

a Surface representation of the cryo-EM maps for the dodecameric, octameric, and DNA-bound tetrameric NrdR structures. b Cartoon representation of the ATP-loaded NrdR tetramer (left) and the dATP/ATP-loaded tetramer (right). Chains A, B, C, and D are colored in beige, green, pink, and blue, respectively. c Interface between the ATP-cones in chain A (beige) and chain B (green) in the ATP-loaded dodecamer and (d) in the dATP/ATP-loaded tetramer. Panels c, d were made from the same perspective, based on an alignment of the ATP-cones in chains A and B in both structures.

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