2pkm

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[[Image:2pkm.jpg|left|200px]]<br /><applet load="2pkm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2pkm.jpg|left|200px]]
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caption="2pkm, resolution 1.90&Aring;" />
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'''Crystal structure of M tuberculosis Adenosine Kinase complexed with adenosine'''<br />
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{{Structure
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|PDB= 2pkm |SIZE=350|CAPTION= <scene name='initialview01'>2pkm</scene>, resolution 1.90&Aring;
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|SITE= <scene name='pdbsite=AC1:Adn+Binding+Site+For+Residue+A+501'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20]
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|GENE= Rv2202 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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}}
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'''Crystal structure of M tuberculosis Adenosine Kinase complexed with adenosine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2PKM 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=ADN:'>ADN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] Known structural/functional Site: <scene name='pdbsite=AC1:Adn+Binding+Site+For+Residue+A+501'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKM OCA].
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2PKM 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=2PKM OCA].
==Reference==
==Reference==
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High resolution crystal structures of Mycobacterium tuberculosis adenosine kinase: insights into the mechanism and specificity of this novel prokaryotic enzyme., Reddy MC, Palaninathan SK, Shetty ND, Owen JL, Watson MD, Sacchettini JC, J Biol Chem. 2007 Sep 14;282(37):27334-42. Epub 2007 Jun 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17597075 17597075]
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High resolution crystal structures of Mycobacterium tuberculosis adenosine kinase: insights into the mechanism and specificity of this novel prokaryotic enzyme., Reddy MC, Palaninathan SK, Shetty ND, Owen JL, Watson MD, Sacchettini JC, J Biol Chem. 2007 Sep 14;282(37):27334-42. Epub 2007 Jun 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17597075 17597075]
[[Category: Adenosine kinase]]
[[Category: Adenosine kinase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: adenosine kinase]]
[[Category: adenosine kinase]]
[[Category: mycobacterium tuberculosis]]
[[Category: mycobacterium tuberculosis]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: tb structural genomics consortium]]
[[Category: tb structural genomics consortium]]
[[Category: tbsgc]]
[[Category: tbsgc]]
[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:14:11 2008''

Revision as of 16:14, 20 March 2008

Image:2pkm.jpg


PDB ID 2pkm

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites:
Ligands:
Gene: Rv2202 (Mycobacterium tuberculosis)
Activity: Adenosine kinase, with EC number 2.7.1.20
Coordinates: save as pdb, mmCIF, xml



Crystal structure of M tuberculosis Adenosine Kinase complexed with adenosine


Overview

Adenosine kinase (ADK) catalyzes the phosphorylation of adenosine (Ado) to adenosine monophosphate (AMP). It is part of the purine salvage pathway that has been identified only in eukaryotes, with the single exception of Mycobacterium spp. Whereas it is not clear if Mycobacterium tuberculosis (Mtb) ADK is essential, it has been shown that the enzyme can selectively phosphorylate nucleoside analogs to produce products toxic to the cell. We have determined the crystal structure of Mtb ADK unliganded as well as ligand (Ado) bound at 1.5- and 1.9-A resolution, respectively. The structure of the binary complexes with the inhibitor 2-fluoroadenosine (F-Ado) bound and with the adenosine 5'-(beta,gamma-methylene)triphosphate (AMP-PCP) (non-hydrolyzable ATP analog) bound were also solved at 1.9-A resolution. These four structures indicate that Mtb ADK is a dimer formed by an extended beta sheet. The active site of the unliganded ADK is in an open conformation, and upon Ado binding a lid domain of the protein undergoes a large conformation change to close the active site. In the closed conformation, the lid forms direct interactions with the substrate and residues of the active site. Interestingly, AMP-PCP binding alone was not sufficient to produce the closed state of the enzyme. The binding mode of F-Ado was characterized to illustrate the role of additional non-bonding interactions in Mtb ADK compared with human ADK.

About this Structure

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

Reference

High resolution crystal structures of Mycobacterium tuberculosis adenosine kinase: insights into the mechanism and specificity of this novel prokaryotic enzyme., Reddy MC, Palaninathan SK, Shetty ND, Owen JL, Watson MD, Sacchettini JC, J Biol Chem. 2007 Sep 14;282(37):27334-42. Epub 2007 Jun 26. PMID:17597075

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