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TitleSolution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From by SAXS and Cryo-Electron Microscopy.
Journal, issue, pagesFront Mol Biosci, Vol. 8, Page 713608, Year 2021
Publish dateJul 26, 2021
AuthorsMahmudul Hasan / Ipsita Banerjee / Inna Rozman Grinberg / Britt-Marie Sjöberg / Derek T Logan /
PubMed AbstractThe essential enzyme ribonucleotide reductase (RNR) is highly regulated both at the level of overall activity and substrate specificity. Studies of class I, aerobic RNRs have shown that overall ...The essential enzyme ribonucleotide reductase (RNR) is highly regulated both at the level of overall activity and substrate specificity. Studies of class I, aerobic RNRs have shown that overall activity is downregulated by the binding of dATP to a small domain known as the ATP-cone often found at the N-terminus of RNR subunits, causing oligomerization that prevents formation of a necessary αβ complex between the catalytic (α) and radical generating (β) subunits. In some relatively rare organisms with RNRs of the subclass NrdAi, the ATP-cone is found at the N-terminus of the β subunit rather than more commonly the α subunit. Binding of dATP to the ATP-cone in β results in formation of an unusual β tetramer. However, the structural basis for how the formation of the active complex is hindered by such oligomerization has not been studied. Here we analyse the low-resolution three-dimensional structures of the separate subunits of an RNR from subclass NrdAi, as well as the αβ octamer that forms in the presence of dATP. The results reveal a type of oligomer not previously seen for any class of RNR and suggest a mechanism for how binding of dATP to the ATP-cone switches off catalysis by sterically preventing formation of the asymmetrical αβ complex.
External linksFront Mol Biosci / PubMed:34381817 / PubMed Central
MethodsEM (single particle)
Resolution8.2 Å
Structure data

EMDB-12985:
Low resolution reconstruction of the dATP-inhibited complex of the ribonucleotide reductase NrdA and NrdB proteins from Leeuwenhoekiella blandensis
Method: EM (single particle) / Resolution: 8.2 Å

Source
  • Leeuwenhoekiella blandensis (bacteria)

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