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Plasmodium Vivax putative polyprenyl pyrophosphate synthase in complex with geranylgeranyl diphosphate
PDB Code 3CC9 Target Class Transferases Target Pv-GGPPS+GGPP Alias n/a Disease Area/Function parasitic disease Date Deposited Feb 25 2008 Authors Related Structure 2IHI
About this structure
Humans and other animals produce IPP and DMAPP via the mevalonic acid (MVA) pathway, which are used to make longer-chained pyrophosphates by enzymes such as farnesyl pyrophosphate synthase (FPPS) and geranylgeranylpyrophosphate synthase. Both of these human enzymes have been characterized and found to profuce strictly one product - respectively FPP and GGPP. The proteins encoded by the gene PF11_0295 and Pv092040 respectively in the Plasmodium falciparum and Plasmodium vivax genomes are sequentially homologous to both human FPPS and GGPPS, but slightly closer to FPPS. Our crystallographic structure of Pv092040 also shows a fold that more closely resembles hFPPS. Interestingly, our experiments show that these proteins from malaria parasites produce GGPPS in biochemical assays.We have previously solved the apo structure of Pv-GGPPS (2IHI). This new structure features GGPP in the active site of the enzyme, clearly showing that in the chain-length determinant region, the presence of alanine and phenylalanine (in green) in place of two phenylalanines in hFPPS permits the longer product to fit.
