Preliminary X-ray crystallographic studies on alcohol dehydrogenase from Drosophila.
The alcohol dehydrogenase (ADHase) enzyme catalyses the oxidation of alcohols to aldehydes or ketones using NAD+ as a cofactor. Functional ADHase from Drosophila lebanonensis is a dimer, with a monomeric molecular weight of 27,000 and with 254 residues in each polypeptide chain. Crystals of the protein have been grown with and without NAD+. Two crystal forms have been observed. Most crystals are plate-like, 0.05 mm in their shortest dimension and up to 0.4 mm in their longest dimension. These crystals are generally too small to diffract efficiently using conventional X-ray sources, so preliminary studies were carried out using the Synchrotron Radiation Source at the SERC Daresbury Laboratory. Twinning was a severe problem with this crystal form. The second form is grown in the absence of NAD+ but with DL-dithiothreitol present. These crystals grow more evenly and diffract to better than 2 A resolution. They are monoclinic, with cell dimensions, a = 81.24(6) A, b = 55.75(4) A, c = 109.60(7) A and beta = 94.26(9) degrees, space group P2(1). There are two dimers in the asymmetric unit, but at low resolution a rotated cell with one dimer per asymmetric unit can be obtained.
Gordon
E J
EJ
Department of Biochemistry, University of Edinburgh, Scotland.
Bury
S M
SM
Sawyer
L
L
Atrian
S
S
Gonzalez-Duarte
R
R
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000818:Animals; D003461:Crystallography; D004330:Drosophila / Q000201:enzymology*; D010315:Particle Accelerators; D014961:X-Ray Diffraction
D000426:Alcohol Dehydrogenase