TY - JOUR
T1 - The prototypic class Ia ribonucleotide reductase from Escherichia coli
T2 - Still surprising after all these years
AU - Brignole, Edward J.
AU - Ando, Nozomi
AU - Zimanyi, Christina M.
AU - Drennan, Catherine L.
PY - 2012/6
Y1 - 2012/6
N2 - RNRs (ribonucleotide reductases) are key players in nucleic acid metabolism, converting ribonucleotides into deoxyribonucleotides. As such, they maintain the intracellular balance of deoxyribonucleotides to ensure the fidelity of DNA replication and repair. The best-studied RNR is the class Ia enzyme from Escherichia coli, which employs two subunits to catalyse its radical-based reaction: β2 houses the diferric-tyrosyl radical cofactor, and α2 contains the active site. Recent applications of biophysical methods to the study of this RNR have revealed the importance of oligomeric state to overall enzyme activity and suggest that unprecedented subunit configurations are in play. Although it has been five decades since the isolation of nucleotide reductase activity in extracts of E. coli, this prototypical RNR continues to surprise us after all these years.
AB - RNRs (ribonucleotide reductases) are key players in nucleic acid metabolism, converting ribonucleotides into deoxyribonucleotides. As such, they maintain the intracellular balance of deoxyribonucleotides to ensure the fidelity of DNA replication and repair. The best-studied RNR is the class Ia enzyme from Escherichia coli, which employs two subunits to catalyse its radical-based reaction: β2 houses the diferric-tyrosyl radical cofactor, and α2 contains the active site. Recent applications of biophysical methods to the study of this RNR have revealed the importance of oligomeric state to overall enzyme activity and suggest that unprecedented subunit configurations are in play. Although it has been five decades since the isolation of nucleotide reductase activity in extracts of E. coli, this prototypical RNR continues to surprise us after all these years.
KW - Allostery
KW - Conformational equilibrium
KW - Feedback regulation
KW - Nucleotide biosynthesis
KW - Oligomerization
KW - Protein-protein interaction
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U2 - 10.1042/BST20120081
DO - 10.1042/BST20120081
M3 - Article
C2 - 22616862
AN - SCOPUS:84861500520
SN - 0300-5127
VL - 40
SP - 523
EP - 530
JO - Biochemical Society Transactions
JF - Biochemical Society Transactions
IS - 3
ER -