Crystallization and preliminary X-ray analysis of the Plasmodium falciparum apicoplast DNA polymerase
Milton, M. E., Choe, J-Y., Honzatko, R. B., & Nelson, S. W. (2015). Crystallization and preliminary X-ray analysis of the Plasmodium falciparum apicoplast DNA polymerase. Acta Crystallographica Section F:Structural Biology Communications, 71, 333-337. DOI: 10.1107/S2053230X15002423
Infection by the parasite Plasmodium falciparum is the leading cause of malaria in humans. The parasite has a unique and essential plastid-like organelle called the apicoplast. The apicoplast contains a genome that undergoes replication and repair through the action of a replicative polymerase (apPOL). apPOL has no direct orthologs in mammalian polymerases and is therefore an attractive antimalarial drug target. No structural information exists for apPOL, and the Klenow fragment of Escherichia coli DNA polymerase I, which is its closest structural homolog, shares only 28% sequence identity. Here, conditions for the crystallization of and preliminary X-ray diffraction data from crystals of P. falciparum apPOL are reported. Data complete to 3.5 angstrom resolution were collected from a single crystal (2 x 2 x 5 mu m) using a 5 mm beam. The space group P6(5)22 (unit-cell parameters a = b = 141.8, c = 149.7 angstrom, alpha = beta = 90, gamma = 120 degrees) was confirmed by molecular replacement. Refinement is in progress.