2BQ1

Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium

Summary for 2BQ1

• Entry DOI: 10.2210/pdb2bq1/pdb
• Related: 1PEM 1PEO 1PEQ 1PEU 1R2F 2R2F
• Descriptor: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 ALPHA SUBUNIT, RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 2 BETA SUBUNIT, 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: r1, r2, r1e, r2f, iron, class 1b, holocomplex, allosteric regulation, ribonucleotide reductase, atp-binding, metal-binding, oxidoreductase, dna replication, radical transfer, allosteric enzyme, asymmetric complex, nucleotide-binding
• Biological source: SALMONELLA TYPHIMURIUM; More
• Total number of polymer chains: 4
• Total formula weight: 235184.75

Authors

Uppsten, M.,Farnegardh, M.,Domkin, V.,Uhlin, U. (deposition date: 2005-04-26, release date: 2006-05-17, Last modification date: 2024-10-16)

Primary citation

Uppsten, M.,Farnegardh, M.,Domkin, V.,Uhlin, U.
The First Holocomplex Structure of Ribonucleotide Reductase Gives New Insight Into its Mechanism of Action
J.Mol.Biol., 359:365-, 2006

PubMed Abstract: Ribonucleotide reductase is an indispensable enzyme for all cells, since it catalyses the biosynthesis of the precursors necessary for both building and repairing DNA. The ribonucleotide reductase class I enzymes, present in all mammals as well as in many prokaryotes and DNA viruses, are composed mostly of two homodimeric proteins, R1 and R2. The reaction involves long-range radical transfer between the two proteins. Here, we present the first crystal structure of a ribonucleotide reductase R1/R2 holocomplex. The biological relevance of this complex is based on the binding of the R2 C terminus in the hydrophobic cleft of R1, an interaction proven to be crucial for enzyme activity, and by the fact that all conserved amino acid residues in R2 are facing the R1 active sites. We suggest that the asymmetric R1/R2 complex observed in the 4A crystal structure of Salmonella typhimurium ribonucleotide reductase represents an intermediate stage in the reaction cycle, and at the moment of reaction the homodimers transiently form a tight symmetric complex.

PubMed: 16631785
DOI: 10.1016/J.JMB.2006.03.035

Experimental method

X-RAY DIFFRACTION (3.99 Å)