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  • Title: Crystallization and preliminary crystallographic analysis of cyanide-insensitive alternative oxidase from Trypanosoma brucei brucei.
    Author: Kido Y, Shiba T, Inaoka DK, Sakamoto K, Nara T, Aoki T, Honma T, Tanaka A, Inoue M, Matsuoka S, Moore A, Harada S, Kita K.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2010 Mar 01; 66(Pt 3):275-8. PubMed ID: 20208159.
    Abstract:
    Cyanide-insensitive alternative oxidase (AOX) is a mitochondrial membrane protein and a non-proton-pumping ubiquinol oxidase that catalyzes the four-electron reduction of dioxygen to water. In the African trypanosomes, trypanosome alternative oxidase (TAO) functions as a cytochrome-independent terminal oxidase that is essential for survival in the mammalian host; hence, the enzyme is considered to be a promising drug target for the treatment of trypanosomiasis. In the present study, recombinant TAO (rTAO) overexpressed in haem-deficient Escherichia coli was purified and crystallized at 293 K by the hanging-drop vapour-diffusion method using polyethylene glycol 400 as a precipitant. X-ray diffraction data were collected at 100 K and were processed to 2.9 A resolution with 93.1% completeness and an overall R(merge) of 9.5%. The TAO crystals belonged to the orthorhombic space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 63.11, b = 136.44, c = 223.06 A. Assuming the presence of two rTAO molecules in the asymmetric unit (2 x 38 kDa), the calculated Matthews coefficient (V(M)) was 3.2 A(3) Da(-1), which corresponds to a solvent content of 61.0%. This is the first report of a crystal of the membrane-bound diiron proteins, which include AOXs.
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