1lio: Difference between revisions

Revision as of 20:59, 2 July 2008

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File:1lio.png

Template:STRUCTURE 1lio

STRUCTURE OF APO T. GONDII ADENOSINE KINASESTRUCTURE OF APO T. GONDII ADENOSINE KINASE

Template:ABSTRACT PUBMED 10801355

About this StructureAbout this Structure

1LIO is a Single protein structure of sequence from Toxoplasma gondii. This structure supersedes the now removed PDB entry 1dh2. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding., Schumacher MA, Scott DM, Mathews II, Ealick SE, Roos DS, Ullman B, Brennan RG, J Mol Biol. 2000 May 19;298(5):875-93. PMID:10801355

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-'''STRUCTURE OF APO T. GONDII ADENOSINE KINASE'''
+===STRUCTURE OF APO T. GONDII ADENOSINE KINASE===
-==Overview==
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-Adenosine kinase (AK) is a key purine metabolic enzyme from the opportunistic parasitic protozoan Toxoplasma gondii and belongs to the family of carbohydrate kinases that includes ribokinase. To understand the catalytic mechanism of AK, we determined the structures of the T. gondii apo AK, AK:adenosine complex and the AK:adenosine:AMP-PCP complex to 2.55 A, 2.50 A and 1.71 A resolution, respectively. These structures reveal a novel catalytic mechanism that involves an adenosine-induced domain rotation of 30 degrees and a newly described anion hole (DTXGAGD), requiring a helix-to-coil conformational change that is induced by ATP binding. Nucleotide binding also evokes a coil-to-helix transition that completes the formation of the ATP binding pocket. A conserved dipeptide, Gly68-Gly69, which is located at the bottom of the adenosine-binding site, functions as the switch for domain rotation. The synergistic structural changes that occur upon substrate binding sequester the adenosine and the ATP gamma phosphate from solvent and optimally position the substrates for catalysis. Finally, the 1.84 A resolution structure of an AK:7-iodotubercidin:AMP-PCP complex reveals the basis for the higher affinity binding of this prodrug over adenosine and thus provides a scaffold for the design of new inhibitors and subversive substrates that target the T. gondii AK.
+The line below this paragraph, {{ABSTRACT_PUBMED_10801355}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10801355}}
 ==About this Structure==
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 [[Category: Scott, D M.]]
 [[Category: Alpha-beta structure]]
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