Structural highlights
Publication Abstract from PubMed3-Hydroxyacyl-CoA dehydrogenase (HAD; EC 1.1.1.35) is the enzyme that catalyzes the third step in fatty-acid beta-oxidation, oxidizing the hydroxyl group of 3-hydroxyacyl-CoA to a keto group. The 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans (cHAD) was cloned, overexpressed in Escherichia coli and purified to homogeneity for crystallography. Initial crystals were obtained by the hanging-drop vapour-diffusion method. Optimization of the precipitant concentration and the pH yielded two types of well diffracting crystals with parallelepiped and cuboid shapes, respectively. Complete diffraction data sets were collected and processed from both crystal types. Preliminary crystallographic analysis indicated that the parallelepiped-shaped crystal belonged to space group P1, while the cuboid-shaped crystal belonged to space group P212121. Analyses of computed Matthews coefficient and self-rotation functions suggested that there are two cHAD molecules in one asymmetric unit in both crystals, forming identical dimers but packing in distinct manners. Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans.,Xu Y, Sun F Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):515-9. doi:, 10.1107/S1744309113007045. Epub 2013 Apr 30. PMID:23695566[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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