This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1pfr
From Proteopedia
|
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
1PFR is a [Single protein] structure of sequence from [Escherichia coli] with FE and HG as [ligands]. Active as [[1]], with EC number [1.17.4.1]. 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
Page seeded by OCA on Mon Oct 29 15:55:20 2007
Categories: Escherichia coli | Single protein | Aberg, A. | Eklund, H. | Hajdu, J. | Logan, D.T. | Nordlund, P. | Regnstrom, K. | Su, X.D. | FE | HG | Acting on ribose 2'-oh | Dna replication | Iron | Oxidoreductase | Reductase
