Crystallization and preliminary X‐ray analysis of the Plasmodium falciparum apicoplast DNA polymerase. Issue 3 (1st March 2015)

• Record Type: Journal Article
• Authors: Milton, Morgan E.; Choe, Jun‐yong; Honzatko, Richard B.; Nelson, Scott W.
• Is Part Of: Acta crystallographica. Volume 71:Issue 3(2015:Mar.)
• Page Start: 333
• Page End: 337
• Publication Date: 2015-03-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15002423
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Infection by the parasite <italic>Plasmodium falciparum</italic> 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 <italic>Escherichia coli</italic> 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 <italic>P. falciparum</italic> 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 <italic>P</italic>6₅22 (unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 141.8, <italic>c</italic> = 149.7 Å, α = β = 90, γ = 120°) was confirmed by molecular replacement. Refinement is in progress.</p> </abstract>