2abs

Crystal structure of T. gondii adenosine kinase complexed with AMP-PCP

spinqualitylabelsall models 2abs, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2abs is a 1 chain structure with sequence from Toxoplasma gondii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: ACP, CL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ADK_TOXGO ATP-dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. It is a key purine metabolic enzyme in the opportunistic parasitic protozoan toxoplasma gondii as it cannot synthesize purines de novo. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The obligate intracellular parasite Toxoplasma gondii is incapable of synthesizing purine nucleotides de novo and relies completely on purines salvaged from the host cells. Adenosine is the preferred precursor and is phosphorylated by adenosine kinase (AK), the most active enzyme in adenosine metabolism in T. gondii. AK thus represents a potential chemotherapeutic target for the treatment of T. gondii infections. The previously solved structures of unliganded AK and AK in complex with adenosine (or 7-iodotubercidin) and an ATP analog revealed a novel catalytic mechanism. A domain closure triggered by a GG switch upon adenosine binding sequesters the adenosine and gamma-phosphate of ATP from the solvent. The formation of the anion hole induced by the ATP binding completes the structural requirements for catalysis. In the current study, the structure of a binary complex of AK and the non-hydrolysable ATP analog AMP-PCP was determined to 1.1 angstroms resolution. The overall structure is similar to the apoenzyme, with an open conformation. AMP-PCP is bound in two relaxed conformations and without anchoring by Arg136. The induced anion hole is the same as that in the ternary complex AK-adenosine-AMP-PCP. This structure provides direct evidence that ATP binding at millimolar concentrations does not require adenosine binding as a prerequisite. Structure of Toxoplasma gondii adenosine kinase in complex with an ATP analog at 1.1 angstroms resolution.,Zhang Y, El Kouni MH, Ealick SE Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):140-5. Epub 2006, Jan 18. PMID:16421444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adenosine kinase 3D structures

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