2pkn: Difference between revisions
New page: left|200px<br /><applet load="2pkn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pkn, resolution 1.90Å" /> '''Crystal structure of... |
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==About this Structure== | ==About this Structure== | ||
2PKN 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=ACP:'>ACP</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKN OCA]. | 2PKN 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=ACP:'>ACP</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:Acp+Binding+Site+For+Residue+A+325'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Sacchettini, J.C.]] | [[Category: Sacchettini, J.C.]] | ||
[[Category: Shetty, N.D.]] | [[Category: Shetty, N.D.]] | ||
[[Category: TBSGC, TB.Structural.Genomics.Consortium.]] | |||
[[Category: Watson, M.D.]] | [[Category: Watson, M.D.]] | ||
[[Category: ACP]] | [[Category: ACP]] | ||
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[[Category: atp]] | [[Category: atp]] | ||
[[Category: mycobacterium tuberculosis]] | [[Category: mycobacterium tuberculosis]] | ||
[[Category: structural genomics]] | |||
[[Category: tb structural genomics consortium]] | |||
[[Category: tbsgc]] | |||
[[Category: transferase]] | |||
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Revision as of 09:18, 13 February 2008
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Crystal structure of M tuberculosis Adenosine Kinase complexed with AMP-PCP (non-hydrolyzable ATP analog)
OverviewOverview
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 StructureAbout this Structure
2PKN is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as Adenosine kinase, with EC number 2.7.1.20 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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