Journal Article

PUBDB-2015-01354

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Recombinant Production, Purification and Crystallization of the Toxoplasma Gondii Coronin WD40 Domain

Kallio, J.>Extern* ; Kursula, I. (Corresponding author)>Extern*EMBL*

2014
Blackwell Oxford [u.a.]

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Please use a persistent id in citations: doi:10.1107/S2053230X14005196

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 $\beta$-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 $\mathit{T}$. $\mathit{gondii}$ 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 $C222_{1}$, with unit-cell parameters $\mathit{a}$ = 55.13, $\mathit{b}$ = 82.51, $\mathit{c}$ = 156.98 Å.

Note: (c) International Union of Crystallography. Post referee full text in progress.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. PETRA Beamline P14 (POF2-54G14) (POF2-54G14)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2014

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Database coverage:
; BIOSIS Previews ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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