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Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit
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2018 (engelsk)Inngår i: eLIFE, E-ISSN 2050-084X, Vol. 7, artikkel-id e31529Artikkel i tidsskrift (Fagfellevurdert) 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.

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ELIFE SCIENCES PUBLICATIONS LTD , 2018. Vol. 7, artikkel-id e31529
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URN: urn:nbn:se:umu:diva-144937DOI: 10.7554/eLife.31529ISI: 000423786200001OAI: oai:DiVA.org:umu-144937DiVA, id: diva2:1185338
Tilgjengelig fra: 2018-02-23 Laget: 2018-02-23 Sist oppdatert: 2018-06-09bibliografisk kontrollert

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Hasan, MahmudulRao Jonna, VenkateswaraHofer, Anders

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