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Recombinant production, purification and crystallization of the Toxoplasma gondii coronin WD40 domain.


ABSTRACT: 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 ?-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 C2221, with unit-cell parameters a = 55.13, b = 82.51, c = 156.98?Å.

SUBMITTER: Kallio JP 

PROVIDER: S-EPMC3976077 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Recombinant production, purification and crystallization of the Toxoplasma gondii coronin WD40 domain.

Kallio Juha Pekka JP   Kursula Inari I  

Acta crystallographica. Section F, Structural biology communications 20140325 Pt 4


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 paras  ...[more]

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