Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+.
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.
School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
Tae-Ho
TH
Jang
School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
Hyun Ho
HH
Park
D002118:Calcium / Q000737:chemistry* / Q000378:metabolism*; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D019204:GTP-Binding Proteins; D006801:Humans; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011503:Transglutaminases / Q000737:chemistry* / Q000378:metabolism*
D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011503:Transglutaminases; D019204:GTP-Binding Proteins; D002118:Calcium
protein cross-linking; transglutaminase 2