3UUS

Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex

3UUS の概要

• エントリーDOI: 10.2210/pdb3uus/pdb
• 分子名称: Ribonucleoside-diphosphate reductase 1 subunit alpha, Ribonucleoside-diphosphate reductase 1 subunit beta, 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: 10 stranded alpha/beta barrel, datp bound, di-iron, oxidoreductase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 521592.01

構造登録者

Zimanyi, C.M.,Drennan, C.L. (登録日: 2011-11-28, 公開日: 2011-12-21, 最終更新日: 2024-11-20)

主引用文献

Ando, N.,Brignole, E.J.,Zimanyi, C.M.,Funk, M.A.,Yokoyama, K.,Asturias, F.J.,Stubbe, J.,Drennan, C.L.
Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase.
Proc.Natl.Acad.Sci.USA, 108:21046-21051, 2011

PubMed Abstract: Essential for DNA biosynthesis and repair, ribonucleotide reductases (RNRs) convert ribonucleotides to deoxyribonucleotides via radical-based chemistry. Although long known that allosteric regulation of RNR activity is vital for cell health, the molecular basis of this regulation has been enigmatic, largely due to a lack of structural information about how the catalytic subunit (α(2)) and the radical-generation subunit (β(2)) interact. Here we present the first structure of a complex between α(2) and β(2) subunits for the prototypic RNR from Escherichia coli. Using four techniques (small-angle X-ray scattering, X-ray crystallography, electron microscopy, and analytical ultracentrifugation), we describe an unprecedented α(4)β(4) ring-like structure in the presence of the negative activity effector dATP and provide structural support for an active α(2)β(2) configuration. We demonstrate that, under physiological conditions, E. coli RNR exists as a mixture of transient α(2)β(2) and α(4)β(4) species whose distributions are modulated by allosteric effectors. We further show that this interconversion between α(2)β(2) and α(4)β(4) entails dramatic subunit rearrangements, providing a stunning molecular explanation for the allosteric regulation of RNR activity in E. coli.

PubMed: 22160671
DOI: 10.1073/pnas.1112715108

実験手法

X-RAY DIFFRACTION (5.65 Å)