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Crystallization and preliminary X‐ray analysis of the Plasmodium falciparum apicoplast DNA polymerase
Author(s) -
Milton Morgan E.,
Choe Junyong,
Honzatko Richard B.,
Nelson Scott W.
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15002423
Subject(s) - apicoplast , biology , plasmodium falciparum , polymerase , dna polymerase , dna polymerase i , plastid , genetics , rna polymerase , genome , dna , apicomplexa , escherichia coli , polymerase chain reaction , malaria , gene , reverse transcriptase , chloroplast , immunology
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 Å resolution were collected from a single crystal (2 × 2 × 5 µm) using a 5 µm beam. The space group P 6 5 22 (unit‐cell parameters a = b = 141.8, c = 149.7 Å, α = β = 90, γ = 120°) was confirmed by molecular replacement. Refinement is in progress.