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Literature summary extracted from

  • Bayse, C.A.; Merz, K.M.
    Mechanistic insights into Mg2+-independent prenylation by CloQ from classical molecular mechanics and hybrid quantum mechanics/molecular mechanics molecular dynamics simulations (2014), Biochemistry, 53, 5034-5041.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.111 molecular mechanics and hybrid quantum mechanics/molecular mechanics molecular dynamics simulations. Positively charged basic residues line the inside of the beta-barrel of CloQ to activate the diphosphate leaving group to replace the function of the Mg(2+) cofactor in other APTases. The effect of the replacement of the Mg(2+) cofactor with basic residues yields a similar activation barrier for prenylation to Mg(2+)-dependent APTases like NphB. The topology of the binding pocket for 4-hydroxyphenylpyruvate is important for selective prenylation at the ortho position of the ring. Methylation at this position alters the conformation of the substrate for O-prenylation at the phenol group Streptomyces roseochromogenus subsp. oscitans

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.111 E281G molecular dynamics simulations Streptomyces roseochromogenus subsp. oscitans
2.5.1.111 F68S molecular dynamics simulations Streptomyces roseochromogenus subsp. oscitans

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.111 Streptomyces roseochromogenus subsp. oscitans Q8GHB2
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Synonyms

EC Number Synonyms Comment Organism
2.5.1.111 CloQ
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 Streptomyces roseochromogenus subsp. oscitans