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Crystal structure of pantoate kinase from Thermococcus kodakarensis
Authors:Akiko Kita  Asako Kishimoto  Takahiro Shimosaka  Hiroya Tomita  Yuusuke Yokooji  Tadayuki Imanaka  Haruyuki Atomi  Kunio Miki
Affiliation:1. Institute for Integrated Radiation and Nuclear Science, Kyoto University, Osaka, Japan;2. Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto, Japan;3. Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto, Japan;4. Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Kusatsu, Japan

JST, CREST, Tokyo, Japan;5. Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto, Japan

JST, CREST, Tokyo, Japan

Abstract:The coenzyme A biosynthesis pathways in most archaea involve two unique enzymes, pantoate kinase and phosphopantothenate synthetase, to convert pantoate to 4′-phosphopantothenate. Here, we report the first crystal structure of pantoate kinase from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complex with ATP and a magnesium ion. The electron density for the adenosine moiety of ATP was very weak, which most likely relates to its broad nucleotide specificity. Based on the structure of the active site that contains a glycerol molecule, the pantoate binding site and the roles of the highly conserved residues are suggested.
Keywords:archaea  CoA biosynthesis  crystal structure  pantoate kinase  Thermococcus kodakarensis
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