Structure of Escherichia coli AdhP (ethanol-inducible dehydrogenase) with bound NAD

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2013-07, Vol.69 (7), p.730-732
• Main Authors: Thomas, Leonard M., Harper, Angelica R., Miner, Whitney A., Ajufo, Helen O., Branscum, Katie M., Kao, Lydia, Sims, Paul A.
• Format: Article
• Language: English
• Subjects: AdhP; Alcohol Dehydrogenase - chemistry; Alcohol Dehydrogenase - genetics; Alcohol Dehydrogenase - metabolism; alcohol dehydrogenases; Amino Acid Sequence; Binding Sites; Catalysis; Catalytic Domain; Crystallization; Crystallography, X-Ray; Escherichia coli; Escherichia coli - enzymology; Ethanol - pharmacology; Models, Molecular; Molecular Sequence Data; NAD - metabolism; Protein Conformation; Protons; Sequence Homology, Amino Acid; Structural Communications; Zinc - chemistry; Zinc - metabolism
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309113015170

The crystal structure of AdhP, a recombinantly expressed alcohol dehydrogenase from Escherichia coli K‐12 (substrain MG1655), was determined to 2.01 Å resolution. The structure, which was solved using molecular replacement, also included the structural and catalytic zinc ions and the cofactor nicotinamide adenine dinucleotide (NAD). The crystals belonged to space group P21, with unit‐cell parameters a = 68.18, b = 118.92, c = 97.87 Å, β = 106.41°. The final R factor and Rfree were 0.138 and 0.184, respectively. The structure of the active site of AdhP suggested a number of residues that may participate in a proton relay, and the overall structure of AdhP, including the coordination to structural and active‐site zinc ions, is similar to those of other tetrameric alcohol dehydrogenase enzymes.