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:
Thermococcus kodakarensis; CoA biosynthesis; archaea; crystal structure; pantoate kinase.
© 2019 Wiley Periodicals, Inc.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / chemistry*
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Archaeal Proteins / metabolism
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Binding Sites
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Cations, Divalent
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Coenzyme A / biosynthesis
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Crystallography, X-Ray
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Gene Expression
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Glycerol / chemistry
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Glycerol / metabolism
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Hydroxybutyrates / chemistry*
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Hydroxybutyrates / metabolism
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Magnesium / chemistry*
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Magnesium / metabolism
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Models, Molecular
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Phosphotransferases / chemistry*
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Phosphotransferases / genetics
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Phosphotransferases / metabolism
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Protein Binding
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Protein Multimerization
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
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Thermococcus / enzymology*
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Thermococcus / genetics
Substances
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Archaeal Proteins
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Cations, Divalent
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Hydroxybutyrates
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Recombinant Proteins
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pantoic acid
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Adenosine Triphosphate
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Phosphotransferases
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Magnesium
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Glycerol
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Coenzyme A