6rme | pdb_00006rme

Structure of IMP bound Plasmodium falciparum IMP-nucleotidase mutant D172N

spinqualitylabelsall models 6rme, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: GOL, IMP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Plasmodium falciparum (Pf) relies solely on the salvage pathway for its purine nucleotide requirements, making this pathway indispensable to the parasite. Purine nucleotide levels are regulated by anabolic processes and by nucleotidases that hydrolyse these metabolites into nucleosides. Certain apicomplexan parasites, including Pf, have an IMP-specific-nucleotidase 1 (ISN1). Here we show, by comprehensive substrate screening, that PfISN1 catalyzes the dephosphorylation of inosine monophosphate (IMP) and is allosterically activated by ATP. Crystal structures of tetrameric PfISN1 reveal complex rearrangements of domain organization tightly associated with catalysis. Immunofluorescence microscopy and expression of GFP-fused protein indicate cytosolic localization of PfISN1 and expression in asexual and gametocyte stages of the parasite. With earlier evidence on isn1 upregulation in female gametocytes, the structures reported in this study may contribute to initiate the design for possible transmission-blocking agents. Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase.,Carrique L, Ballut L, Shukla A, Varma N, Ravi R, Violot S, Srinivasan B, Ganeshappa UT, Kulkarni S, Balaram H, Aghajari N Nat Commun. 2020 Jun 26;11(1):3228. doi: 10.1038/s41467-020-17013-x. PMID:32591529 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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