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Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones

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Author

  • Renzo Johansson
  • Venkateswara Rao Jonna
  • Rohit Kumar
  • Niloofar Nayeri
  • Daniel Lundin
  • Britt Marie Sjöberg
  • Anders Hofer
  • Derek T. Logan

Summary, in English

Summary Ribonucleotide reductases (RNRs) reduce ribonucleotides to deoxyribonucleotides. Their overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures. The crystal structure and solution X-ray scattering data of a novel dATP-induced homotetramer of the Pseudomonas aeruginosa class I RNR reveal the structural bases for its unique properties, namely one ATP cone that binds two dATP molecules and a second one that is non-functional, binding no nucleotides. Mutations in the observed tetramer interface ablate oligomerization and dATP-induced inhibition but not the ability to bind dATP. Sequence analysis shows that the novel type of ATP cone may be widespread in RNRs. The present study supports a scenario in which diverse mechanisms for allosteric activity regulation are gained and lost through acquisition and evolutionary erosion of different types of ATP cone.

Publishing year

2016-06-07

Language

English

Pages

906-917

Publication/Series

Structure

Volume

24

Issue

6

Document type

Journal article

Publisher

Cell Press

Topic

  • Structural Biology

Status

Published

ISBN/ISSN/Other

  • ISSN: 0969-2126