Complexes of Escherichia coli Adenylate Kinase and Nucleotides:1H NMR Studies 
of the Nucleotide Sites in Solution

Vetter, Ingrid R.; Reinstein, Jochen; Rösch, Paul

doi:10.1021/bi00484a015

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Complexes of Escherichia coli Adenylate Kinase and Nucleotides:1H NMR Studies of the Nucleotide Sites in Solution

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Reinstein, Jochen
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Rösch, Paul
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Vetter, I. R., Reinstein, J., & Rösch, P. (1990). Complexes of Escherichia coli Adenylate Kinase and Nucleotides:1H NMR Studies of the Nucleotide Sites in Solution. Biochemistry, 29(32), 7459-7467. doi:10.1021/bi00484a015.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-ACEE-9

Zusammenfassung

One- and two-dimensional nuclear magnetic resonance (NMR) studies, in particular substrate--protein nuclear Overhauser effect (NOESY) measurements, as well as nucleotide and P1,P5-bis-(5'-adenosyl) pentaphosphate (AP5A) titrations and studies of the temperature-dependent unfolding of the tertiary structure of Escherichia coli adenylate kinase (AKEC) were performed. These experiments and comparison with the same type of experiments performed with the porcine enzyme [Rösch, P., Klaus, W., Auer, M., & Goody, R. S. (1989) Biochemistry 28, 4318-4325] led us to the following conclusions: (1) At pH 8 and concentrations of approximately 2.5-3 mM, AKEC is partially unfolded at 318 K. (2) ATP.Mg2+ binds to the ATP site with a dissociation constant of approximately 40 microM under the assumption that ATP binds to one nucleotide site only. (3) AP5A.Mg2+ binds to both nucleotide sites and thus simulates the active complex. (4) The ATP.Mg2+ adenine in the AKEC.AP5A.Mg2+ complex is located close to His134 and Phe19. (5) The AKEC "G-loop" with bound ATP.Mg2+ is structurally highly homologous to the loop region in the oncogene product p21 with bound GTP.Mg2+.