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Crystal structure of pantoate kinase from Thermococcus kodakarensis
Author(s) -
Kita Akiko,
Kishimoto Asako,
Shimosaka Takahiro,
Tomita Hiroya,
Yokooji Yuusuke,
Imanaka Tadayuki,
Atomi Haruyuki,
Miki Kunio
Publication year - 2020
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25852
Subject(s) - thermococcus , biochemistry , archaea , active site , chemistry , transferase , enzyme , moiety , stereochemistry , biology , gene
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.