2R1R

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI

2R1R の概要

• エントリーDOI: 10.2210/pdb2r1r/pdb
• 分子名称: RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN, THYMIDINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: ribonucleotide reductase, deoxyribonucleotide synthesis, radical chemistry, allosteric regulation, specificity, complex (oxidoreductase-peptide), complex (oxidoreductase-peptide) complex, complex (oxidoreductase/peptide)
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 268163.33

構造登録者

Eriksson, M.,Eklund, H. (登録日: 1997-07-21, 公開日: 1998-01-28, 最終更新日: 2024-10-16)

主引用文献

Eriksson, M.,Uhlin, U.,Ramaswamy, S.,Ekberg, M.,Regnstrom, K.,Sjoberg, B.M.,Eklund, H.
Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding.
Structure, 5:1077-1092, 1997

PubMed Abstract: Ribonucleotide reductase (RNR) is an essential enzyme in DNA synthesis, catalyzing all de novo synthesis of deoxyribonucleotides. The enzyme comprises two dimers, termed R1 and R2, and contains the redox active cysteine residues, Cys462 and Cys225. The reduction of ribonucleotides to deoxyribonucleotides involves the transfer of free radicals. The pathway for the radical has previously been suggested from crystallographic results, and is supported by site-directed mutagenesis studies. Most RNRs are allosterically regulated through two different nucleotide-binding sites: one site controls general activity and the other controls substrate specificity. Our aim has been to crystallographically demonstrate substrate binding and to locate the two effector-binding sites.

PubMed: 9309223
DOI: 10.1016/S0969-2126(97)00259-1

実験手法

X-RAY DIFFRACTION (3 Å)