1xik

From Proteopedia

Revision as of 06:20, 30 October 2007

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN

Overview

BACKGROUND. Ribonucleotide reductases (RNRs) catalyze the formation of the, deoxyribonucleotides that are essential for DNA synthesis. The R2 subunit, of Escherichia coli RNR is a homodimer containing one dinuclear iron, centre per monomer. A tyrosyl radical is essential for catalysis, and is, formed via a reaction in which the reduced, diferrous form of the iron, centre activates dioxygen. To help understand the mechanism of oxygen, activation, we examined the structure of the diferrous form of R2., RESULTS. The crystal structures of reduced forms of both wild type R2 and, a mutant of R2 (Ser211--> Ala) have been determined at 1.7 A and 2.2 A, resolution, respectively. The diferrous iron centre was compared to the, previously determined structure of the oxidized, diferric form of R2. ... [(full description)]

About this Structure

1XIK is a [Single protein] structure of sequence from [Escherichia coli] with FE2 and HG as [ligands]. Active as [Oxidoreductase], with EC number [1.17.4.1]. Structure known Active Sites: FE1 and FE2. Full crystallographic information is available from [OCA].

Reference

Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site., Logan DT, Su XD, Aberg A, Regnstrom K, Hajdu J, Eklund H, Nordlund P, Structure. 1996 Sep 15;4(9):1053-64. PMID:8805591

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