Structural properties of homodimeric quinoprotein ethanol deyhdrogenase from

@inproceedings{Goerisch2000StructuralPO,
  title={Structural properties of homodimeric quinoprotein ethanol deyhdrogenase from},
  author={H. Goerisch and T. Keitel and A. Diehl and T. Knaute and Z. Dauter and W. Hoehne},
  year={2000}
}
The X-ray structure of the periplasmic quinoprotein ethanol dehydrogenase (QEDH) fromPseudomonas aeruginosashows a homodimer, where each subunit forms a disk-shaped super-barrel composed of eight antiparallel twisted s-sheets, arranged in a propeller-like fashion. The s-propeller fold is stabilized by a repetitive Ala/Trp/Gly docking motif, which is modified in four of the eight docking contacts. The overall folding of the polypeptide is very similar to that known for the large α-subunit of the… Expand
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Transcriptional regulation of the acetyl-CoA synthetase gene acsA in Pseudomonas aeruginosa
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