| PMID : |
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 (16672241) |
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| titre : |
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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. |
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| auteur(s) : |
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Marco Bellinzoni1, Ahmed Haouz2, Martin Graña1, Hélène Munier-Lehmann3, William Shepard4, Pedro Maria Alzari ( ) 1, 2 |
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| laboratoire : |
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| résumé : |
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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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langue du texte
intégral : |
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Anglais |
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| ISSN : |
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0961-8368 |
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| type de publication : |
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Articles dans des revues avec comité de lecture |
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| DOI : |
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10.1110/ps.062163406 |
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| journal : |
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| Protein Science (Protein Sci) |
| Publisher |
Wiley-Blackwell |
| ISSN |
0961-8368 (eISSN : 1469-896X) |
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| Audience : |
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internationale |
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| date de publication : |
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06/2006 |
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| volume : |
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15 |
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| numéro : |
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6 |
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| page, identifiant, ... : |
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1489-93 |
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| Descripteur(s) MeSH : |
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Adenosine Diphosphate – Adenosine Triphosphate – Adenylate Kinase – Binding Sites – Catalysis – Crystallography – X-Ray – Magnesium – Models – Molecular – Mycobacterium tuberculosis – Protein Conformation |
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