6MVE

Reduced X-ray crystal structure of Bacillus subtilis ribonucleotide reductase NrdE alpha subunit with TTP, ATP, and ADP

6MVE の概要

• エントリーDOI: 10.2210/pdb6mve/pdb
• 関連するPDBエントリー: 6MT9 6MV9
• 分子名称: Ribonucleoside-diphosphate reductase, THYMIDINE-5'-TRIPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: ribonucleotide reductase, allostery, nucleotide metabolism, datp, atp, oxidoreductase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 82232.32

構造登録者

Thomas, W.C.,Brooks, F.P.,Bacik, J.P.,Ando, N. (登録日: 2018-10-25, 公開日: 2019-06-19, 最終更新日: 2023-10-11)

主引用文献

Thomas, W.C.,Brooks 3rd, F.P.,Burnim, A.A.,Bacik, J.P.,Stubbe, J.,Kaelber, J.T.,Chen, J.Z.,Ando, N.
Convergent allostery in ribonucleotide reductase.
Nat Commun, 10:2653-2653, 2019

PubMed Abstract: 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 organism Bacillus 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.

PubMed: 31201319
DOI: 10.1038/s41467-019-10568-4

実験手法

X-RAY DIFFRACTION (2.55 Å)