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Literature summary for 1.1.1.86 extracted from

  • Wong, S.H.; Lonhienne, T.G.; Winzor, D.J.; Schenk, G.; Guddat, L.W.
    Bacterial and plant ketol-acid reductoisomerases have different mechanisms of induced fit during the catalytic cycle (2012), J. Mol. Biol., 424, 168-179.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with Mg2+ and NADPH at 2.3 A resolution. The binding of Mg2+ increases structural disorder while the binding of NADPH increases the structural rigidity of the enzyme. The binding of Mg2+ and NADPH opens the interface between the N- and C-domains, thereby allowing access for the substrates to bind Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the coordination geometry for Mg(1) is approximately octahedral, with three water ligands and three protein ligands, the carboxylate groups of D217, E389 and E393. Mg(2) is seven coordinate with six waters and a carboxylate oxygen from D217. A dissociation constant of about 500 microM applies to the interaction of Mg2+ with unliganded enzyme. In presence of NADPH the Kd increases to about 800 microM Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52428
-
4 * 52428, calculated Escherichia coli
228000
-
sedimentation equilibrium analysis Escherichia coli
230000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P05793
-
-

Subunits

Subunits Comment Organism
tetramer 4 * 52428, calculated Escherichia coli

Synonyms

Synonyms Comment Organism
KARI
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH binding of NADPH is enthalpy driven. NADPH binding may have an opposing effect to that of Mg2+ binding by inducing an increase in structural stability Escherichia coli