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Crystallization and Preliminary X-ray Crystallographic Studies of Transglutaminase 2 in Complex with Ca2+

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Specialty Chemistry
Date 2014 Apr 5
PMID 24699752
Citations 1
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Abstract

Transglutaminase 2 (TG2) is a multi-functional protein that has been implicated in a variety of physiological cellular activities, including apoptosis, angiogenesis and cellular differentiation. Two functions of TG2 are protein cross-linking and GTP hydrolysis activities. The protein cross-linking activity of TG2 is positively controlled by calcium; however, the molecular mechanism of its Ca(2+)-dependent activity is completely unknown. In the present study, full-length human TG2 in complex with Ca(2+) was overexpressed, purified and crystallized at 20°C as a first step towards elucidating this mechanism. X-ray diffraction data were collected to a resolution of 3.4 Å from a crystal belonging to space group C2221, with unit-cell parameters a = 133.08, b = 216.30, c = 166.26 Å. Based on these data, the asymmetric unit was estimated to contain three molecules.

Citing Articles

Competitive Binding of Magnesium to Calcium Binding Sites Reciprocally Regulates Transamidase and GTP Hydrolysis Activity of Transglutaminase 2.

Jeong E, Lee K, Kim G, Kim C, Lee J, Kim H Int J Mol Sci. 2020; 21(3).

PMID: 31991788 PMC: 7037829. DOI: 10.3390/ijms21030791.

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