Disruption of an oligomeric interface prevents allosteric inhibition of Escherichia coli class Ia ribonucleotide reductase.

ABSTRACT: Ribonucleotide reductases (RNRs) convert ribonucleotides to deoxynucleotides, a process essential for DNA biosynthesis and repair. Class Ia RNRs require two dimeric subunits for activity: an α₂ subunit that houses the active site and allosteric regulatory sites and a β₂ subunit that houses the diferric tyrosyl radical cofactor. Ribonucleotide reduction requires that both subunits form a compact α₂β₂ state allowing for radical transfer from β₂ to α₂ RNR activity is regulated allosterically by dATP, which inhibits RNR, and by ATP, which restores activity. For the well-studied Escherichia coli class Ia RNR, dATP binding to an allosteric site on α promotes formation of an α₄β₄ ring-like state. Here,

SUBMITTER: Chen PY 

PROVIDER: S-EPMC6028975 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature