dc.contributor.author | Thomas, Leonard M. | |
dc.contributor.author | Harper, Angelica R. | |
dc.contributor.author | Miner, Whitney A. | |
dc.contributor.author | Ajufo, Helen O. | |
dc.contributor.author | Branscum, Katie M. | |
dc.contributor.author | Kao, Lydia | |
dc.contributor.author | Sims, Paul A. | |
dc.date.accessioned | 2014-04-25T19:09:04Z | |
dc.date.accessioned | 2016-03-30T15:33:57Z | |
dc.date.available | 2014-04-25T19:09:04Z | |
dc.date.available | 2016-03-30T15:33:57Z | |
dc.date.issued | 2013 | |
dc.identifier.issn | 1744-3091 | |
dc.identifier.uri | https://hdl.handle.net/11244/10332 | |
dc.description.abstract | The 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.language | en_US | en_US |
dc.publisher | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | |
dc.relation.isbasedon | http://journals.iucr.org/f/issues/2013/07/00/tt5041/index.html | |
dc.subject | Chemistry, Biochemistry. | en_US |
dc.title | Structure of Escherichia coli AdhP (ethanol-inducible dehydrogenase) with bound NAD | en_US |
dc.type | Article | en_US |
dc.description.peerreview | Yes | en_US |
dc.description.peerreviewnotes | The manuscript was peer-reviewed by two anonymous reviewers. | en_US |
dc.identifier.doi | 10.1107/S1744309113015170 | en_US |