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![Illustration of the intricate organization of the PKA structure, wherein different parts of the protein are connected through elaborate hydrogen bonding networks (dashed yellow lines), glued together by the hydrophobic assemblies (light blue and orange volumes)—all working together to build the functional active site. Insert shows protonation of the transferred phosphoryl group (cyan mesh) and its many interactions with water and the active site amino acid residues. Credit: Jill Hemman/ORNL](/sites/default/files/styles/list_page_thumbnail/public/2019-03/19-G00204_MR_graphic_Kovalevsky_proof5_2.png?h=b7fbb1a9&itok=wrZFNX-o)
OAK RIDGE, Tenn., March 20, 2019—Direct observations of the structure and catalytic mechanism of a prototypical kinase enzyme—protein kinase A or PKA—will provide researchers and drug developers with significantly enhanced abilities to understand and treat fatal diseases and neurological disorders such as cancer, diabetes, and cystic fibrosis.
Scientists studying a valuable, but vulnerable, species of poplar have identified the genetic mechanism responsible for the species’ inability to resist a pervasive and deadly disease. Their finding, published in the Proceedings of the National Academy of Sciences, could lead to more successful hybrid poplar varieties for increased biofuels and forestry production and protect native trees against infection.
![Methanotroph_OB3b_cells Methanotroph_OB3b_cells](/sites/default/files/styles/list_page_thumbnail/public/Methanotroph_OB3b_cells_2.jpg?itok=Iml9vTIS)
A team led by the Department of Energy’s Oak Ridge National Laboratory has identified a novel microbial process that can break down toxic methylmercury in the environment, a fundamental scientific discovery that could potentially reduce mercury toxicity levels and sup...