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Literature summary for 2.7.7.9 extracted from

  • Roeben, A.; Plitzko, J.M.; Koerner, R.; Boettcher, U.M.; Siegers, K.; Hayer-Hartl, M.; Bracher, A.
    Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae (2006), J. Mol. Biol., 364, 551-560.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
both in solution and crystal, enzyme forms homooctamers. Association of octamers is mediated by left-handed helices in the C-terminal domains forming a toroidal solenoid structure. The catalytic domains do not directly contact each other, consistent with simple Michaelis-Menten kinetics Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
isoform Ugp1
-

Subunits

Subunits Comment Organism
octamer crystallization data Saccharomyces cerevisiae