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.

中文翻译：

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柯达热球菌泛酸激酶的晶体结构。

在大多数古细菌中，辅酶A的生物合成途径涉及两种独特的酶，泛酸激酶和磷酸泛酸合成酶，以将泛酸转化为4'-磷酸泛酸。在这里，我们报道了来自超嗜热古细菌，柯达氏嗜热球菌的泛酸激酶的第一个晶体结构，以及它与ATP和镁离子的复合物。ATP腺苷部分的电子密度很弱，这很可能与它的宽核苷酸特异性有关。基于包含甘油分子的活性位点的结构，提出了泛酸酯结合位点和高度保守残基的作用。