1dgm

CRYSTAL STRUCTURE OF ADENOSINE KINASE FROM TOXOPLASMA GONDII

spinqualitylabelsall models 1dgm, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dgm is a 1 chain structure with sequence from Toxgo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACY, ADN, CL, MG Activity: Adenosine kinase, with EC number 2.7.1.20 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 Human infection with Toxoplasma gondii is an important cause of morbidity and mortality. Protozoan parasites such as T. gondii are incapable of de novo purine biosynthesis and must acquire purines from their host, so the purine salvage pathway offers a number of potential targets for antiparasitic chemotherapy. In T. gondii tachyzoites, adenosine is the predominantly salvaged purine nucleoside, and thus adenosine kinase is a key enzyme in the purine salvage pathway of this parasite. The structure of T. gondii adenosine kinase was solved using molecular replacement and refined by simulated annealing at 1.8 A resolution to an R-factor of 0.214. The overall structure and the active site geometry are similar to human adenosine kinase, although there are significant differences. The T. gondii adenosine kinase has several unique features compared to the human sequence, including a five-residue deletion in one of the four linking segments between the two domains, which is probably responsible for a major change in the orientation of the two domains with respect to each other. These structural differences suggest the possibility of developing specific inhibitors of the parasitic enzyme. Crystal structure of adenosine kinase from Toxoplasma gondii at 1.8 A resolution.,Cook WJ, DeLucas LJ, Chattopadhyay D Protein Sci. 2000 Apr;9(4):704-12. PMID:10794412 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adenosine kinase 3D structures

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