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Literature summary for 1.17.4.1 extracted from

  • Xu, H.; Faber, C.; Uchiki, T.; Fairman, J.W.; Racca, J.; Dealwis, C.
    Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation (2006), Proc. Natl. Acad. Sci. USA, 103, 4022-4027.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
alpha subunit, in apo form, in complex with AMP analogue 5'-adenylyl-beta,gamma-imidodiphosphate, with 5'-adenylyl-beta,gamma-imidodiphosphate and CDP, with 5'-adenylyl-beta,gamma-imidodiphosphate and UDP, with dGTP and ADP, TTP and GDP. Binding of specificity effector rearranges loop 2 and moves residue P294 out of the catalytic site, accomodating substrate binding. substrate binding further rearranges loop2. Cross-talk occurs largely through R293 and Q288 of loop 2. Substrate ribose binds with its 3’ hydroxyl closer than its 2’ hydroxyl to residue C218 of the catalytic redox pair Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P21524
-
-

Reaction

Reaction Comment Organism Reaction ID
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin binding of specificity effector rearranges loop 2 and moves residue P294 out of the catalytic site, accomodating substrate binding. substrate binding further rearranges loop2. Cross-talk occurs largely through R293 and Q288 of loop 2. Substrate ribose binds with its 3’ hydroxyl closer than its 2’ hydroxyl to residue C218 of the catalytic redox pair Saccharomyces cerevisiae
a