6jbc

Phosphotransferase related to CoA biosynthesis pathway

spinqualitylabelsall models 6jbc, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jbc is a 1 chain structure with sequence from Thermococcus kodakarensis KOD1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: CA, EDO, GOL, NA, PG4, PPV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function POK_THEKO Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway (PubMed:19666462, PubMed:22865846). Displays broad nucleotide specificity and utilizes ATP, GTP, UTP, and CTP with comparable catalytic efficiencies (PubMed:22865846). Publication Abstract from PubMed 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. Crystal structure of pantoate kinase from Thermococcus kodakarensis.,Kita A, Kishimoto A, Shimosaka T, Tomita H, Yokooji Y, Imanaka T, Atomi H, Miki K Proteins. 2020 May;88(5):718-724. doi: 10.1002/prot.25852. Epub 2019 Nov 20. PMID:31697438 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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