2cdn

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{{STRUCTURE_2cdn| PDB=2cdn | SCENE= }}
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'''CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ADENYLATE KINASE COMPLEXED WITH TWO MOLECULES OF ADP AND MG'''
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===CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ADENYLATE KINASE COMPLEXED WITH TWO MOLECULES OF ADP AND MG===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 16672241 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16672241}}
==About this Structure==
==About this Structure==
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[[Category: Phosphoryl transfer]]
[[Category: Phosphoryl transfer]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:53:43 2008''

Revision as of 18:53, 28 July 2008


PDB ID 2cdn

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2cdn, resolution 1.90Å ()
Ligands: ,
Activity: Adenylate kinase, with EC number 2.7.4.3
Related: 1p4s
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ADENYLATE KINASE COMPLEXED WITH TWO MOLECULES OF ADP AND MG

Template:ABSTRACT PUBMED 16672241

About this Structure

2CDN is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The crystal structure of Mycobacterium tuberculosis adenylate kinase in complex with two molecules of ADP and Mg2+ supports an associative mechanism for phosphoryl transfer., Bellinzoni M, Haouz A, Grana M, Munier-Lehmann H, Shepard W, Alzari PM, Protein Sci. 2006 Jun;15(6):1489-93. Epub 2006 May 2. PMID:16672241

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