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Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases
Authors:WeiShen Aik  Michael A McDonough  Armin Thalhammer  Rasheduzzaman Chowdhury  Christopher J Schofield
Institution:1. Program in Chemical Biology, University of Michigan, Ann Arbor, MI 48109, USA;2. Laboratory of Computational Chemistry and Biochemistry, Swiss Federal Institute of Technology, Lausanne, Switzerland;3. Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA;4. Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA;1. Biocenter Oulu, Faculty of Biochemistry and Molecular Medicine, Oulu Center for Cell-Matrix Research, University of Oulu, FIN-90014 Oulu, Finland;2. Department of Chemistry, University of Utah, Salt Lake City, UT 84112, USA
Abstract:.
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  • Highlights? Structural features of 2OG oxygenases involved in substrate recognition are analyzed. ? Crystallographic studies reveal the versatility of the jelly roll fold in substrate binding. ? Defined structural regions that interact with substrate(s) are biased by fold topology. ? The utility of the enzyme–substrate structures for engineering and selective inhibition are discussed.
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