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

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...

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Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2014-09, Vol.70 (9), p.1280-1283
Main Authors: Lee, Jee Un, Son, Ji Young, Yoo, Ki-Young, Shin, Woori, Im, Dong-Won, Kim, Seung Jun, Ryu, Seong Eon, Heo, Yong-Seok
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Crystallization
Crystallization Communications
Crystallography, X-Ray - methods
DNA Primers
Humans
Molecular Sequence Data
MTMR4
myotubularin-related proteins
PH-GRAM domain
phosphatase
phosphoinositide
Protein Conformation
Protein Tyrosine Phosphatases, Non-Receptor - chemistry
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Summary: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.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X14017658