Literature summary for 2.7.4.3 extracted from

Aden, J.; Wolf-Watz, M.
NMR identification of transient complexes critical to adenylate kinase catalysis (2007), J. Am. Chem. Soc., 129, 14003-14012.

Crystallization (Commentary)

Crystallization (Comment)	Organism
solution-state NMR approach to probe the native energy landscape of adenylate kinase in its free form, in complex with its natural substrates, and in the presence of a tight binding inhibitor. Binding of ATP induces a dynamic equilibrium in which the ATP binding motif populates both the open and the closed conformations with almost equal populations. A similar scenario is observed for AMP binding, which induces an equilibrium between open and closed conformations of the AMP binding motif. Simultaneous binding of AMP and ATP is required to force both substrate binding motifs to close cooperatively. Unidirectional energetic coupling between the ATP and AMP binding sites	Escherichia coli

Crystallization (Comment)

Organism

solution-state NMR approach to probe the native energy landscape of adenylate kinase in its free form, in complex with its natural substrates, and in the presence of a tight binding inhibitor. Binding of ATP induces a dynamic equilibrium in which the ATP binding motif populates both the open and the closed conformations with almost equal populations. A similar scenario is observed for AMP binding, which induces an equilibrium between open and closed conformations of the AMP binding motif. Simultaneous binding of AMP and ATP is required to force both substrate binding motifs to close cooperatively. Unidirectional energetic coupling between the ATP and AMP binding sites

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P69441	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + AMP = 2 ADP	binding of ATP induces a dynamic equilibrium in which the ATP binding motif populates both the open and the closed conformations with almost equal populations. A similar scenario is observed for AMP binding, which induces an equilibrium between open and closed conformations of the AMP binding motif. Simultaneous binding of AMP and ATP is required to force both substrate binding motifs to close cooperatively. Unidirectional energetic coupling between the ATP and AMP binding sites	Escherichia coli	a

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Release 2023.1 (January 2023)