Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 69, Issue -, Pages 730-732Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309113015170
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Funding
- Center of Biomedical Research Excellence (CoBRE) award from the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health [P20GM103640]
- University of Oklahoma
- NIGMS [P41-GM103311]
- Direct For Biological Sciences
- Div Of Biological Infrastructure [0922269] Funding Source: National Science Foundation
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The crystal structure of AdhP, a recombinantly expressed alcohol dehydrogenase from Escherichia coli K-12 (substrain MG1655), was determined to 2.01 angstrom 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 P2(1), with unit-cell parameters a = 68.18, b = 118.92, c = 97.87 angstrom, 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.
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