Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4.

ABSTRACT: Phosphoinositide lipid molecules play critical roles in intracellular signalling pathways and are regulated by phospholipases, lipid kinases and phosphatases. In particular, phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate are related to endosomal trafficking events through the recruitment of effector proteins and are involved in the degradation step of autophagy. Myotubularin-related proteins (MTMRs) are a large family of phosphatases that catalyze the dephosphorylation of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate at the D3 position, thereby regulating cellular phosphoinositide levels. In this study, the PH-GRAM domain of human MTMR4 was cloned, overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method. The crystals diffracted to 3.20?Å resolution at a synchrotron beamline and belonged to either space group P61 or P65, with unit-cell parameters a = b = 109.10, c = 238.97?Å.

SUBMITTER: Lee JU 

PROVIDER: S-EPMC4157437 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature