Unknown

Dataset Information

0

Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+.


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.

SUBMITTER: Jang TH 

PROVIDER: S-EPMC3976076 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+.

Jang Tae-Ho TH   Park Hyun Ho HH  

Acta crystallographica. Section F, Structural biology communications 20140325 Pt 4


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  ...[more]

Similar Datasets

| S-EPMC3151120 | biostudies-literature
| S-EPMC2805548 | biostudies-literature
| S-EPMC2593703 | biostudies-literature
| S-EPMC3606571 | biostudies-literature
| S-EPMC4188092 | biostudies-literature
| S-EPMC2225176 | biostudies-literature
| S-EPMC3087642 | biostudies-literature
| S-EPMC4304759 | biostudies-literature
| S-EPMC2917292 | biostudies-literature
| S-EPMC4118811 | biostudies-literature