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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-ACEE-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-6A04-3
Genre: Journal Article

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Biochem_29_1990_7459.pdf (Any fulltext), 994KB
 
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Vetter, Ingrid R., Author
Reinstein, Jochen1, Author              
Rösch, Paul2, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: 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+.

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Language(s): eng - English
 Dates: 1989-08-161990-04-021990-08-01
 Publication Status: Published in print
 Pages: 9
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 Rev. Type: Peer
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 29 (32) Sequence Number: - Start / End Page: 7459 - 7467 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103