Recombinant production, purification and crystallization of the Toxoplasma gondii coronin WD40 domain. Issue 4 (1st April 2014)

• Record Type: Journal Article
• Authors: Kallio, Juha Pekka; Kursula, Inari
• Is Part Of: Acta crystallographica. Volume 70:Issue 4(2014:Apr.)
• Page Start: 517
• Page End: 521
• Publication Date: 2014-04-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14005196
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Toxoplasma gondii</italic> 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 &gt;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 <italic>T. gondii</italic> 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 <italic>C</italic>222₁, with unit‐cell parameters <italic>a</italic> = 55.13, <italic>b</italic> = 82.51, <italic>c</italic> = 156.98 Å.</p> </abstract>