How ATP and dATP Act as Molecular Switches to Regulate Enzymatic Activity in the Prototypical Bacterial Class Ia Ribonucleotide Reductase.

ABSTRACT: Class Ia ribonucleotide reductases (RNRs) are allosterically regulated by ATP and dATP to maintain the appropriate deoxyribonucleotide levels inside the cell for DNA biosynthesis and repair. RNR activity requires precise positioning of the β₂ and α₂ subunits for the transfer of a catalytically essential radical species. Excess dATP inhibits RNR through the creation of an α-β interface that restricts the ability of β₂ to obtain a position that is capable of radical transfer. ATP breaks the α-β interface, freeing β₂ and restoring enzyme activity. Here, we investigate the molecular basis for allosteric activity regulation in the well-studied Escherichia coli class Ia RNR through the determination of six crystal structures and accompanying bio

SUBMITTER: Funk MA 

PROVIDER: S-EPMC11447812 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature