Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From Leeuwenhoekiella blandensis by SAXS and Cryo-Electron Microscopy

Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From Leeuwenhoekiella blandensis by SAXS and Cryo-Electron Microscopy

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 th...

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Bibliographic Details
Main Authors: Mahmudul Hasan, Ipsita Banerjee, Inna Rozman Grinberg, Britt-Marie Sjöberg, Derek T. Logan
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-07-01
Series:Frontiers in Molecular Biosciences
Subjects:
ribonucleotide reductase
allosteric regulation
oligomerization
nucleotide binding
small-angle X-ray scattering
single particle cryo-EM
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2021.713608/full

Internet

https://www.frontiersin.org/articles/10.3389/fmolb.2021.713608/full

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