4GKV

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

Summary for 4GKV

• Entry DOI: 10.2210/pdb4gkv/pdb
• Descriptor: Alcohol dehydrogenase, propanol-preferring, cleaved peptide fragment corresponding to the C-terminal His tag, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 146033.58

Authors

Sims, P.A.,Thomas, L.M.,Harper, A.R.,Miner, W.A.,Ajufo, H.O.,Branscrum, K.M.,Kao, L. (deposition date: 2012-08-13, release date: 2013-07-10, Last modification date: 2024-02-28)

Primary citation

Thomas, L.M.,Harper, A.R.,Miner, W.A.,Ajufo, H.O.,Branscum, K.M.,Kao, L.,Sims, P.A.
Structure of Escherichia coli AdhP (ethanol-inducible dehydrogenase) with bound NAD.
Acta Crystallogr.,Sect.F, 69:730-732, 2013

PubMed 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, 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.

PubMed: 23832197
DOI: 10.1107/S1744309113015170

Experimental method

X-RAY DIFFRACTION (2.008 Å)