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Recombinant production, purification and crystallization of the Toxoplasma gondii coronin WD40 domain
Author(s) -
Kallio Juha Pekka,
Kursula Inari
Publication year - 2014
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/s2053230x14005196
Subject(s) - actin , toxoplasma gondii , apicomplexa , biology , myosin , gliding motility , microneme , microbiology and biotechnology , recombinant dna , cytoskeleton , coiled coil , cytokinesis , actin cytoskeleton , motility , biochemistry , cell division , genetics , gene , cell , plasmodium falciparum , antibody , malaria , immunology
Toxoplasma gondii is one of the most widely spread parasitic organisms in the world. Together with other apicomplexan parasites, it utilizes a special actin–myosin motor for its cellular movement, called gliding motility. This actin‐based process is regulated by a small set of actin‐binding proteins, which in Apicomplexa comprises only 10–15 proteins, compared with >150 in higher eukaryotes. Coronin is a highly conserved regulator of the actin cytoskeleton, but its functions, especially in parasites, have remained enigmatic. Coronins consist of an N‐terminal actin‐binding β‐propeller WD40 domain, followed by a conserved region, and a C‐terminal coiled‐coil domain implicated in oligomerization. Here, the WD40 domain and the conserved region of coronin from T. gondii were produced recombinantly and crystallized. A single‐wavelength diffraction data set was collected to a resolution of 1.65 Å. The crystal belonged to the orthorhombic space group C 222 1 , with unit‐cell parameters a = 55.13, b = 82.51, c = 156.98 Å.