Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase

Journal of Molecular Biology
Anselm Erich OberholzerBernhard Erni

Abstract

Dihydroxyacetone (Dha) kinases are a family of sequence-related enzymes that utilize either ATP or phosphoenolpyruvate (PEP) as source of high energy phosphate. The PEP-dependent Dha kinase of Escherichia coli consists of three subunits. DhaK and DhaL are homologous to the Dha and nucleotide-binding domains of the ATP-dependent kinase of Citrobacter freundii. The DhaM subunit is a multiphosphorylprotein of the PEP:sugar phosphotransferase system (PTS). DhaL contains a tightly bound ADP as coenzyme that gets transiently phosphorylated in the double displacement of phosphate between DhaM and Dha. Here we report the 2.6A crystal structure of the E.coli DhaL subunit. DhaL folds into an eight-helix barrel of regular up-down topology with a hydrophobic core made up of eight interlocked aromatic residues and a molecule of ADP bound at the narrower end of the barrel. The alpha and beta phosphates of ADP are complexed by two Mg2+ and by a hydrogen bond to the imidazole ring of an invariant histidine. The Mg ions in turn are coordinated by three gamma-carboxyl groups of invariant aspartate residues. Water molecules complete the octahedral coordination sphere. The nucleotide is capped by an alpha-helical segment connecting helices 7 and 8...Continue Reading

References

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Citations

Jan 7, 2011·Proceedings of the National Academy of Sciences of the United States of America·Rong ShiIrena Ekiel
Jul 9, 2014·Proceedings of the National Academy of Sciences of the United States of America·Joshua B ParsonsCharles O Rock
Oct 30, 2008·The Journal of Biological Chemistry·Andreas ZurbriggenBernhard Erni
Mar 7, 2019·International Journal of Molecular Sciences·Joaquim Rui RodriguesJoão Meireles Ribeiro

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