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

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Title
Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4
Author(s)
J U Lee; J Y Son; K Y Yoo; W Shin; D W Im; Seung Jun Kim; S E Ryu; Y S Heo
Bibliographic Citation
Acta Crystallographica Section F-Structural Biology, vol. 70, no. 9, pp. 1280-1283
Publication Year
2014
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 A 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 A.
Keyword
MTMR4myotubularin-related proteinsPH-GRAM domainphosphatasephosphoinositide
ISSN
1744-3091
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S2053230X14017658
Type
Article
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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