5CNS

Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to CDP and dATP at 2.97 Angstroms resolution

5CNS の概要

• エントリーDOI: 10.2210/pdb5cns/pdb
• 関連するPDBエントリー: 5CNT 5CNU 5CNV
• 分子名称: Ribonucleoside-diphosphate reductase 1 subunit alpha, Ribonucleoside-diphosphate reductase 1 subunit beta, CYTIDINE-5'-DIPHOSPHATE, ... (8 entities in total)
• 機能のキーワード: allostery, substrate specificity, ribonucleotide reductase, nucleotide metabolism, oxidoreductase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 523143.23

構造登録者

Chen, P.Y.-T.,Zimanyi, C.M.,Funk, M.A.,Drennan, C.L. (登録日: 2015-07-18, 公開日: 2016-01-20, 最終更新日: 2023-09-27)

主引用文献

Zimanyi, C.M.,Chen, P.Y.,Kang, G.,Funk, M.A.,Drennan, C.L.
Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli.
Elife, 5:e07141-e07141, 2016

PubMed Abstract: Ribonucleotide reductase (RNR) converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair. This enzyme is responsible for reducing all four ribonucleotide substrates, with specificity regulated by the binding of an effector to a distal allosteric site. In all characterized RNRs, the binding of effector dATP alters the active site to select for pyrimidines over purines, whereas effectors dGTP and TTP select for substrates ADP and GDP, respectively. Here, we have determined structures of Escherichia coli class Ia RNR with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how RNR 'reads' the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell.

PubMed: 26754917
DOI: 10.7554/eLife.07141

実験手法

X-RAY DIFFRACTION (2.975 Å)