Crystal structure of C-terminally tagged apo-UbiD from E. coli

Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis.

3-octaprenyl-4-hydroxybenzoate carboxy-lyase

Polyprenyl p-hydroxybenzoate decarboxylase

Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

Crystals grown in 0.1 mM SPG pH 8, 25 w/v PEG 1500 Crystals were cryo-protected using 10 PEG 400 in mother liquor followed by rapid cryocooling.

Biotechnology and Biological Sciences Research Council

HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT

3-octaprenyl-4-hydroxybenzoate carboxy-lyase (E.C.4.1.1.98)

UbiD, decarboxylase, ubiquinone biosynthesis, prFMN binding, Lyase