Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones
(2016) In Structure 24(6). p.906-917- Abstract
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... (More)
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.
(Less)
- author
- Johansson, Renzo
LU
; Jonna, Venkateswara Rao
; Kumar, Rohit
LU
; Nayeri, Niloofar
; Lundin, Daniel
; Sjöberg, Britt Marie
; Hofer, Anders
and Logan, Derek T.
LU
- organization
- publishing date
- 2016-06-07
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Structure
- volume
- 24
- issue
- 6
- pages
- 12 pages
- publisher
- Cell Press
- external identifiers
-
- scopus:84964594794
- pmid:27133024
- wos:000377782200011
- ISSN
- 0969-2126
- DOI
- 10.1016/j.str.2016.03.025
- language
- English
- LU publication?
- yes
- id
- 8888abe5-8991-468e-9dcd-a9ebcff6b05a
- date added to LUP
- 2016-10-04 15:06:17
- date last changed
- 2024-08-10 20:18:09
@article{8888abe5-8991-468e-9dcd-a9ebcff6b05a, abstract = {{<p>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.</p>}}, author = {{Johansson, Renzo and Jonna, Venkateswara Rao and Kumar, Rohit and Nayeri, Niloofar and Lundin, Daniel and Sjöberg, Britt Marie and Hofer, Anders and Logan, Derek T.}}, issn = {{0969-2126}}, language = {{eng}}, month = {{06}}, number = {{6}}, pages = {{906--917}}, publisher = {{Cell Press}}, series = {{Structure}}, title = {{Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones}}, url = {{http://dx.doi.org/10.1016/j.str.2016.03.025}}, doi = {{10.1016/j.str.2016.03.025}}, volume = {{24}}, year = {{2016}}, }