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Journal articles
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.
https://hal-pasteur.archives-ouvertes.fr/pasteur-00166948
Contributor : Hélène Munier-Lehmann Connect in order to contact the contributor
Submitted on : Monday, August 13, 2007 - 4:11:10 PM
Last modification on : Monday, January 10, 2022 - 11:44:05 AM
Contributor : Hélène Munier-Lehmann Connect in order to contact the contributor
Submitted on : Monday, August 13, 2007 - 4:11:10 PM
Last modification on : Monday, January 10, 2022 - 11:44:05 AM
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