2a9z: Difference between revisions

Revision as of 15:58, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2a9z.png

Template:STRUCTURE 2a9z

Crystal structure of T. gondii adenosine kinase complexed with N6-dimethyladenosine and AMP-PCPCrystal structure of T. gondii adenosine kinase complexed with N6-dimethyladenosine and AMP-PCP

Template:ABSTRACT PUBMED 17242506

About this StructureAbout this Structure

2A9Z is a Single protein structure of sequence from Toxoplasma gondii. Full crystallographic information is available from OCA.

ReferenceReference

Substrate analogs induce an intermediate conformational change in Toxoplasma gondii adenosine kinase., Zhang Y, El Kouni MH, Ealick SE, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):126-34. Epub 2007, Jan 16. PMID:17242506

Page seeded by OCA on Sun Jul 27 15:58:39 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2a9z.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2a9z|  PDB=2a9z  |  SCENE=  }}
-'''Crystal structure of T. gondii adenosine kinase complexed with N6-dimethyladenosine and AMP-PCP'''
+===Crystal structure of T. gondii adenosine kinase complexed with N6-dimethyladenosine and AMP-PCP===
-==Overview==
+<!--
-Adenosine kinase (AK) is a key enzyme in purine metabolism in the ubiquitous intracellular parasite Toxoplasma gondii and is a potential chemotherapeutic target for the treatment of T. gondii infections. To better understand the structure-activity relationship of 6-substituted purine ribosides, the structures of the T. gondii AK-N6,N6-dimethyladenosine (DMA) complex, the AK-DMA-AMP-PCP complex, the AK-6-methyl mercaptopurine riboside (MMPR) complex and the AK-MMPR-AMP-PCP complex were determined to 1.35, 1.35, 1.75 and 1.75 A resolution, respectively. These structures reveal a conformation intermediate between open and closed, with a small lid-domain rotation of 12 degrees . Residues Gly143-X-X-Gly146 undergo torsional changes upon substrate binding, which together with a Gly68-Gly69 switch induces a hinge bending of the lid domain. The intermediate conformation suggests that ATP binding is independent of adenosine binding. Orienting the gamma-phosphate group of ATP into the optimal catalytic position may be the last step before the onset of chemical catalysis and may require the translocation of Arg136 following the complete closure of the lid domain. 6-Substituted purine-nucleoside analogs are accommodated in a hydrophobic cavity. Modification at the N6 or C6 position of the nucleoside would affect the interactions with the surrounding residues and the binding affinity.
+The line below this paragraph, {{ABSTRACT_PUBMED_17242506}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17242506 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17242506}}
 ==About this Structure==
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 [[Category: Intermediate conformation]]
 [[Category: Ribokinase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:47:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:58:39 2008''