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

ABSTRACT: 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, ? = 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.

SUBMITTER: Thomas LM

PROVIDER: S-EPMC3702314 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

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

Thomas Leonard M LM Harper Angelica R AR Miner Whitney A WA Ajufo Helen O HO Branscum Katie M KM Kao Lydia L Sims Paul A PA

Acta crystallographica. Section F, Structural biology and crystallization communications 20130627 Pt 7

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 0.18 ...[more]

PMID: 23832197

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