5IM3

Crystal structure of the class I ribonucleotide reductase from Pseudomonas aeruginosa in complex with dATP

Summary for 5IM3

• Entry DOI: 10.2210/pdb5im3/pdb
• Descriptor: Ribonucleoside-diphosphate reductase, 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, allosteric regulation, ten-stranded alpha-beta barrel, atp cone
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
• Total number of polymer chains: 2
• Total formula weight: 217458.00

Authors

Johansson, R.,Logan, D.T. (deposition date: 2016-03-05, release date: 2016-05-04, Last modification date: 2024-11-06)

Primary citation

Johansson, R.,Jonna, V.R.,Kumar, R.,Nayeri, N.,Lundin, D.,Sjoberg, B.M.,Hofer, A.,Logan, D.T.
Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones.
Structure, 24:906-917, 2016

PubMed Abstract: 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.

PubMed: 27133024
DOI: 10.1016/j.str.2016.03.025

Experimental method

X-RAY DIFFRACTION (2.298 Å)