1PFR

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN

Summary for 1PFR

• Entry DOI: 10.2210/pdb1pfr/pdb
• Descriptor: PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE, FE (III) ION, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: reductase, oxidoreductase, dna replication, iron, acting on ribose 2'-oh
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 81003.87

Authors

Logan, D.T.,Su, X.D.,Aberg, A.,Regnstrom, K.,Hajdu, J.,Eklund, H.,Nordlund, P. (deposition date: 1996-12-03, release date: 1997-03-12, Last modification date: 2024-05-22)

Primary citation

Logan, D.T.,Su, X.D.,Aberg, A.,Regnstrom, K.,Hajdu, J.,Eklund, H.,Nordlund, P.
Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site.
Structure, 4:1053-1064, 1996

PubMed Abstract: 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.

PubMed: 8805591
DOI: 10.1016/S0969-2126(96)00112-8

Experimental method

X-RAY DIFFRACTION (2.2 Å)