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Crystallization and preliminary X‐ray crystallographic analysis of the PH‐GRAM domain of human MTMR4
Author(s) -
Lee Jee Un,
Son Ji Young,
Yoo KiYoung,
Shin Woori,
Im DongWon,
Kim Seung Jun,
Ryu Seong Eon,
Heo YongSeok
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14017658
Subject(s) - phosphatidylinositol , phosphatase , dephosphorylation , microbiology and biotechnology , kinase , biochemistry , effector , chemistry , biology , crystallography , phosphorylation
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 P 6 1 or P 6 5 , with unit‐cell parameters a = b = 109.10, c = 238.97 Å.