Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family.

@article{Aufhammer2004CoenzymeBI,
  title={Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family.},
  author={Stephan W Aufhammer and Eberhard Warkentin and Holger Berk and Seigo Shima and Rudolf Kurt Thauer and Ulrich Ermler},
  journal={Structure},
  year={2004},
  volume={12 3},
  pages={361-70}
}
F(420)-dependent secondary alcohol dehydrogenase (Adf) from methanogenic archaea is a member of the growing bacterial luciferase family which are all TIM barrel enzymes, most of which with an unusual nonprolyl cis peptide bond. We report here on the crystal structure of Adf from Methanoculleus thermophilicus at 1.8 A resolution in complex with a F(420)-acetone adduct. The knowledge of the F(420) binding mode in Adf provides the molecular basis for modeling F(420) and FMN into the other enzymes… CONTINUE READING

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