Convergent allostery in ribonucleotide reductase.
Convergent allostery in ribonucleotide reductase.
复制标题
核糖核苷酸还原酶的趋同变构。
DOI：
10.1038/s41467-019-10568-4
复制
发表时间：
2019
影响因子：
16.6
通讯作者：
Ando,Nozomi
中科院分区：
文献类型：
--
作者：
Thomas,WilliamC;Brooks3rd,FPhil;Burnim,AudreyA;Bacik,John-Paul;Stubbe,JoAnne;Kaelber,JasonT;Chen,JamesZ;Ando,Nozomi
Ribonucleotide reductases (RNRs) use a conserved radical-based mechanism to catalyze the conversion of ribonucleotides to deoxyribonucleotides. Within the RNR family, class Ib RNRs are notable for being largely restricted to bacteria, including many pathogens, and for lacking an evolutionarily mobile ATP-cone domain that allosterically controls overall activity. In this study, we report the emergence of a distinct and unexpected mechanism of activity regulation in the sole RNR of the model organismBacillus subtilis. Using a hypothesis-driven structural approach that combines the strengths of small-angle X-ray scattering (SAXS), crystallography, and cryo-electron microscopy (cryo-EM), we describe the reversible interconversion of six unique structures, including a flexible active tetramer and two inhibited helical filaments. These structures reveal the conformational gymnastics necessary for RNR activity and the molecular basis for its control via an evolutionarily convergent form of allostery.
