Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.17.4.1 extracted from

  • Ando, N.; Brignole, E.J.; Zimanyi, C.M.; Funk, M.A.; Yokoyama, K.; Asturias, F.J.; Stubbe, J.; Drennan, C.L.
    Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase (2011), Proc. Natl. Acad. Sci. USA, 108, 21046-21051.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of a complex between alpha2 and beta2 subunits forming an unprecedented alpha4beta4 ring-like structure in the presence of the negative activity effector dATP, while the active conformation is alpha2beta2. Under physiological conditions, the enzyme exists as a mixture of transient alpha2beta2 and alpha4beta4 species whose distributions are modulated by allosteric effectors. This interconversion between entails dramatic subunit rearrangements Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P00452 isoform NrdA
-

Subunits

Subunits Comment Organism
More a complex between alpha2 and beta2 subunits forms an unprecedented alpha4beta4 ring-like structure in the presence of the negative activity effector dATP, while the active conformation is alpha2beta2. Under physiological conditions, the enzyme exists as a mixture of transient alpha2beta2 and alpha4beta4 species whose distributions are modulated by allosteric effectors. This interconversion between entails dramatic subunit rearrangements Escherichia coli

Synonyms

Synonyms Comment Organism
NrdA
-
Escherichia coli