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Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-8779-6464
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Lund University, Sweden.ORCID iD: 0000-0002-1767-6440
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Number of Authors: 13
2018 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 7, article id e31529Article in journal (Refereed) Published
Abstract [en]

Ribonucleotide reductases (RNRs) are key enzymes in DNA metabolism, with allosteric mechanisms controlling substrate specificity and overall activity. In RNRs, the activity master-switch, the ATP-cone, has been found exclusively in the catalytic subunit. In two class I RNR subclasses whose catalytic subunit lacks the ATP-cone, we discovered ATP-cones in the radical-generating subunit. The ATP-cone in the Leeuwenhoekiella blandensis radical-generating subunit regulates activity via quaternary structure induced by binding of nucleotides. ATP induces enzymatically competent dimers, whereas dATP induces non-productive tetramers, resulting in different holoenzymes. The tetramer forms by interactions between ATP-cones, shown by a 2.45 A crystal structure. We also present evidence for an (MnMnIV)-Mn-III metal center. In summary, lack of an ATP-cone domain in the catalytic subunit was compensated by transfer of the domain to the radical-generating subunit. To our knowledge, this represents the first observation of transfer of an allosteric domain between components of the same enzyme complex.

Place, publisher, year, edition, pages
2018. Vol. 7, article id e31529
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Biological Sciences
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URN: urn:nbn:se:su:diva-153793DOI: 10.7554/eLife.31529ISI: 000423786200001OAI: oai:DiVA.org:su-153793DiVA, id: diva2:1190659
Available from: 2018-03-15 Created: 2018-03-15 Last updated: 2018-03-15Bibliographically approved

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Rozman Grinberg, InnaLundin, DanielHasan, MahmudulLoderer, ChrishtophSahlin, MargaretaSjöberg, Britt-Marie
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