2CDN

Crystal structure of Mycobacterium tuberculosis adenylate kinase complexed with two molecules of ADP and Mg

Summary for 2CDN

• Entry DOI: 10.2210/pdb2cdn/pdb
• Related: 1P4S
• Descriptor: ADENYLATE KINASE, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: adenylate kinase, phosphoryl transfer, associative mechanism, atp-binding, kinase, nucleotide biosynthesis, nucleotide-binding, transferase
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Cellular location: Cytoplasm: P69440
• Total number of polymer chains: 1
• Total formula weight: 23202.98

Authors

Bellinzoni, M.,Haouz, A.,Grana, M.,Munier-Lehmann, H.,Alzari, P.M. (deposition date: 2006-01-25, release date: 2006-05-10, Last modification date: 2023-12-13)

Primary citation

Bellinzoni, M.,Haouz, A.,Grana, M.,Munier-Lehmann, H.,Shepard, W.,Alzari, P.M.
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 Sci., 15:1489-, 2006

PubMed 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.

PubMed: 16672241
DOI: 10.1110/PS.062163406

Experimental method

X-RAY DIFFRACTION (1.9 Å)