TY  - JOUR
AU  - Kallio, Juha
AU  - Kursula, Inari
TI  - Recombinant Production, Purification and Crystallization of the Toxoplasma Gondii Coronin WD40 Domain
JO  - Acta crystallographica / F
VL  - 70
SN  - 1744-3091
CY  - Oxford [u.a.]
PB  - Blackwell
M1  - PUBDB-2015-01354
SP  - 517-521
PY  - 2014
N1  - (c) International Union of Crystallography. Post referee full text in progress.
AB  - 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 <i>T</i>. <i>gondii</i> 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 C222<sub>1</sub>, with unit-cell parameters <i>a</i> = 55.13, <i>b</i> = 82.51, <i>c</i> = 156.98 Å.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000333757800026
C6  - pmid:24699753
DO  - DOI:10.1107/S2053230X14005196
UR  - https://bib-pubdb1.desy.de/record/207456
ER  -