3bf3 is a 6 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[COAX_THEMA] Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Pantothenate kinase (PanK) catalyzes the first step of the universal five-step coenzyme A (CoA) biosynthetic pathway. The recently characterized type III PanK (PanK-III, encoded by the coaX gene) is distinct in sequence, structure and enzymatic properties from both the long-known bacterial type I PanK (PanK-I, exemplified by the Escherichia coli CoaA protein) and the predominantly eukaryotic type II PanK (PanK-II). PanK-III enzymes have an unusually high Km for ATP, are resistant to feedback inhibition by CoA, and are unable to utilize the N-alkylpantothenamide family of pantothenate analogues as alternative substrates, thus making type III PanK ineffective in generating CoA analogues as antimetabolites in vivo. Previously, we reported the crystal structure of the PanK-III from Thermotoga maritima and identified it as a member of the "acetate and sugar kinase/heat shock protein 70/actin" (ASKHA) superfamily. Here we report the crystal structures of the same PanK-III in complex with one of its substrates (pantothenate), its product (phosphopantothenate) as well as a ternary complex structure of PanK-III with pantothenate and ADP. These results are combined with isothermal titration calorimetry experiments to present a detailed structural and thermodynamic characterization of the interactions between PanK-III and its substrates ATP and pantothenate. Comparison of substrate binding and catalytic sites of PanK-III with that of eukaryotic PanK-II revealed drastic differences in the binding modes for both ATP and pantothenate substrates, and suggests that these differences may be exploited in the development of new inhibitors specifically targeting PanK-III.
Structural basis for substrate binding and the catalytic mechanism of type III pantothenate kinase.,Yang K, Strauss E, Huerta C, Zhang H Biochemistry. 2008 Feb 5;47(5):1369-80. Epub 2008 Jan 11. PMID:18186650[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Yang K, Eyobo Y, Brand LA, Martynowski D, Tomchick D, Strauss E, Zhang H. Crystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria. J Bacteriol. 2006 Aug;188(15):5532-40. PMID:16855243 doi:188/15/5532
↑Yang K, Strauss E, Huerta C, Zhang H. Structural basis for substrate binding and the catalytic mechanism of type III pantothenate kinase. Biochemistry. 2008 Feb 5;47(5):1369-80. Epub 2008 Jan 11. PMID:18186650 doi:10.1021/bi7018578
