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Crystal structure of pantoate kinase from Thermococcus kodakarensis |
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| 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 |