Formation of a complex containing ATP, Mg2+, and spermine. Structural evidence and biological significance

• Published in: The Journal of biological chemistry Vol. 273; no. 47; pp. 30939 - 30944
• Main Authors: Meksuriyen, D, Fukuchi-Shimogori, T, Tomitori, H, Kashiwagi, K, Toida, T, Imanari, T, Kawai, G, Igarashi, K
• Format: Journal Article
• Language: English
• Published: United States 20.11.1998
• Subjects: Adenosine Triphosphate - chemistry; Adenosine Triphosphate - metabolism; ATP-Binding Cassette Transporters; Binding Sites; Carrier Proteins - drug effects; Cations, Divalent; Cyclic AMP-Dependent Protein Kinases - drug effects; Escherichia coli Proteins; Magnesium - chemistry; Magnesium - metabolism; Membrane Proteins - drug effects; Molecular Conformation; Nuclear Magnetic Resonance, Biomolecular; Phosphorus Isotopes; Spermine - chemistry; Spermine - metabolism; Spermine - pharmacology

The conformation of ATP in the presence of Mg2+ and/or spermine was studied by 31P and 1H NMR, to clarify how polyamines interact with ATP. Spermine predominantly interacted with the beta- and gamma-phosphates of ATP in the presence of Mg2+. A conformational change of the beta- and gamma-phosphate o...