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Literature summary for 1.17.4.1 extracted from

  • Zimanyi, C.M.; Chen, P.Y.; Kang, G.; Funk, M.A.; Drennan, C.L.
    Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli (2016), eLife, 5, e07141 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.4.1

Activating Compound

Activating Compound Comment Organism Structure
dATP the binding of effector dATP alters the active site to select for pyrimidines over purines. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell Escherichia coli
dGTP the binding of effector dGTP alters the active site to select for ADP and GDP. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell Escherichia coli
TTP the binding of effector TTP alters the active site to select for ADP and GDP. Crystal structures of Escherichia coli class Ia ribonucleotide reductase with all four substrate/specificity effector-pairs bound (CDP/dATP, UDP/dATP, ADP/dGTP, GDP/TTP) that reveal the conformational rearrangements responsible for this remarkable allostery. These structures delineate how ribonucleotide reductase reads the base of each effector and communicates substrate preference to the active site by forming differential hydrogen bonds, thereby maintaining the proper balance of deoxynucleotides in the cell Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are grown using the hanging drop vapor diffusion technique Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + thioredoxin Escherichia coli the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair 2'-dADP + thioredoxin disulfide + H2O
-
 ?
CDP + thioredoxin Escherichia coli the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair 2'-dCDP + thioredoxin disulfide + H2O
-
 ?
UDP + thioredoxin Escherichia coli the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair 2'-dUDP + thioredoxin disulfide + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P00452 and P69924 P00452: subunit NrdA, P69924: subunit NrdB
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + thioredoxin
-
 Escherichia coli 2'-dADP + thioredoxin disulfide + H2O
-
 ?
ADP + thioredoxin the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli 2'-dADP + thioredoxin disulfide + H2O
-
 ?
CDP + thioredoxin
-
 Escherichia coli 2'-dCDP + thioredoxin disulfide + H2O
-
 ?
CDP + thioredoxin the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli 2'-dCDP + thioredoxin disulfide + H2O
-
 ?
UDP + thioredoxin
-
 Escherichia coli 2'-dUDP + thioredoxin disulfide + H2O
-
 ?
UDP + thioredoxin the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli 2'-dUDP + thioredoxin disulfide + H2O
-
 ?

Synonyms

Synonyms Comment Organism
class Ia RNR
-
 Escherichia coli
ribonucleotide reductase
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair Escherichia coli