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

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dc.contributor.authorThomas, Leonard M.
dc.contributor.authorHarper, Angelica R.
dc.contributor.authorMiner, Whitney A.
dc.contributor.authorAjufo, Helen O.
dc.contributor.authorBranscum, Katie M.
dc.contributor.authorKao, Lydia
dc.contributor.authorSims, Paul A.
dc.date.accessioned2014-04-25T19:09:04Z
dc.date.accessioned2016-03-30T15:33:57Z
dc.date.available2014-04-25T19:09:04Z
dc.date.available2016-03-30T15:33:57Z
dc.date.issued2013
dc.description.abstractThe crystal structure of AdhP, a recombinantly expressed alcohol dehydrogenase from Escherichia coli K-12 (substrain MG1655), was determined to 2.01 angstroms 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 angstroms, beta = 106.41 degrees. The final R-factor and R-free 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.en_US
dc.description.peerreviewYesen_US
dc.description.peerreviewnotesThe manuscript was peer-reviewed by two anonymous reviewers.en_US
dc.identifier.doi10.1107/S1744309113015170en_US
dc.identifier.issn1744-3091
dc.identifier.urihttp://hdl.handle.net/11244/10332
dc.languageen_USen_US
dc.publisherActa Crystallographica Section F: Structural Biology and Crystallization Communications
dc.relation.isbasedonhttp://journals.iucr.org/f/issues/2013/07/00/tt5041/index.html
dc.subjectChemistry, Biochemistry.en_US
dc.titleStructure of Escherichia coli AdhP (ethanol-inducible dehydrogenase) with bound NADen_US
dc.typeArticleen_US

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