Ribonucleotide reductase large subunit, N-terminal
Short name | RNR_lsu_N |
Overlapping homologous superfamilies |
Description
References
1.Structure-function studies of the large subunit of ribonucleotide reductase from Escherichia coli. Nilsson O, Lundqvist T, Hahne S, Sjoberg BM. Biochem. Soc. Trans. 16, 91-4, (1988). PMID: 3286319
2.From RNA to DNA, why so many ribonucleotide reductases? Reichard P. Science 260, 1773-7, (1993). View articlePMID: 8511586
3.The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer. Sintchak MD, Arjara G, Kellogg BA, Stubbe J, Drennan CL. Nat. Struct. Biol. 9, 293-300, (2002). View articlePMID: 11875520
4.Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnstrom K, Sjoberg BM, Eklund H. Structure 5, 1077-92, (1997). View articlePMID: 9309223
5.Structure of ribonucleotide reductase protein R1. Uhlin U, Eklund H. Nature 370, 533-9, (1994). View articlePMID: 8052308
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- Pfam:PF00317