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The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer.

Abstract : The crystal structure of Mycobacterium tuberculosis adenylate kinase (MtAK) in complex with two ADP molecules and Mg2+ has been determined at 1.9 A resolution. Comparison with the solution structure of the enzyme, obtained in the absence of substrates, shows significant conformational changes of the LID and NMP-binding domains upon substrate binding. The ternary complex represents the state of the enzyme at the start of the backward reaction (ATP synthesis). The structure is consistent with a direct nucleophilic attack of a terminal oxygen from the acceptor ADP molecule on the beta-phosphate from the donor substrate, and both the geometry and the distribution of positive charge in the active site support the hypothesis of an associative mechanism for phosphoryl transfer.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-00166948
Contributor : Hélène Munier-Lehmann <>
Submitted on : Monday, August 13, 2007 - 4:11:10 PM
Last modification on : Monday, January 13, 2020 - 5:08:07 PM

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Marco Bellinzoni, Ahmed Haouz, Martin Graña, Hélène Munier-Lehmann, William Shepard, et al.. The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer.. Protein Science, Wiley, 2006, 15 (6), pp.1489-93. ⟨10.1110/ps.062163406⟩. ⟨pasteur-00166948⟩

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