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Published online before print May 2, 2006, 10.1110/ps.062163406
Protein Science (2006), 15:1489-1493. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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PROTEIN STRUCTURE REPORT

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

Marco Bellinzoni1, Ahmed Haouz2, Martin Graña1, Hélène Munier-Lehmann3, William Shepard4 and Pedro M. Alzari1,2

1 Unité de Biochimie Structurale
2 Plate-forme de Cristallogenèse et Diffraction des Rayons-X
3 Unité de Chimie Organique, CNRS-URA 2185, Institut Pasteur, F-75724 Paris, France
4 Synchrotron Soleil, L'Orme de Merisiers, Saint Aubin BP48, 91192 Gif sur Yvette, France

(RECEIVED February 15, 2006; FINAL REVISION February 15, 2006; ACCEPTED February 22, 2006)

The crystal structure of Mycobacterium tuberculosis adenylate kinase (MtAK) in complex with two ADP molecules and Mg2+ has been determined at 1.9 Å 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.

Keywords: adenylate kinase; phosphoryl transfer; X-ray crystallography; associative mechanism; Mycobacterium tuberculosis


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