Ribonucleotide reductases (RNRs) catalyze the conversion of nucleoside diphosphates to deoxynucleotides de novo supplying and controlling the ratios and amounts of dNTP pools essential in DNA replication and DNA repair.  The class Ia RNRs (found in humans and <i>E.coli</i>) are composed of two weakly interacting subunits alpha and beta, that form an active/asymmetric (a2b2) and an organism specific inactive (a4b4, a6, fibrils) states depending on the dNTPs, dATP, and ATP and other small molecules. Recent biophysical studies including Crystallography, SAXS, AUC, SEC and negative stain & cryoEM are providing a picture of how this flexible machine functions to control (deoxy)nucleotide pools and plays an important role in the fidelity of these processes. These studies have revealed the importance of quaternary structure in the inactivation of RNR by the clinically used drugs gemcitabine and clofarabine.  A summary of our current understanding and the next RNR frontiers will be discussed.<br/> <br/>

Frontiers in ribonucleotide reductases: nucleotide-dependent control of quaternary structure and enzyme activity

2019 Spring National Meeting

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