2cdn

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[[Image:2cdn.gif|left|200px]]<br /><applet load="2cdn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cdn.gif|left|200px]]
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caption="2cdn, resolution 1.90&Aring;" />
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'''CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ADENYLATE KINASE COMPLEXED WITH TWO MOLECULES OF ADP AND MG'''<br />
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{{Structure
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|PDB= 2cdn |SIZE=350|CAPTION= <scene name='initialview01'>2cdn</scene>, resolution 1.90&Aring;
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|SITE= <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ADENYLATE KINASE COMPLEXED WITH TWO MOLECULES OF ADP AND MG'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CDN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] Known structural/functional Site: <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDN OCA].
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2CDN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDN OCA].
==Reference==
==Reference==
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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., 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16672241 16672241]
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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., 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:[http://www.ncbi.nlm.nih.gov/pubmed/16672241 16672241]
[[Category: Adenylate kinase]]
[[Category: Adenylate kinase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:14:10 2008''

Revision as of 14:14, 20 March 2008


PDB ID 2cdn

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites:
Ligands: and
Activity: Adenylate kinase, with EC number 2.7.4.3
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

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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