Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4
- Authors
- Lee, Jee Un; Son, Ji Young; Yoo, Ki-Young; Shin, Woori; Im, Dong-Won; Kim, Seung Jun; Ryu, Seong Eon; Heo, Yong-Seok
- Issue Date
- Sep-2014
- Publisher
- INT UNION CRYSTALLOGRAPHY
- Keywords
- MTMR4; myotubularin-related proteins; PH-GRAM domain; phosphatase; phosphoinositide
- Citation
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.1280 - 1283
- Indexed
- SCIE
SCOPUS
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
- Volume
- 70
- Start Page
- 1280
- End Page
- 1283
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/159209
- DOI
- 10.1107/S2053230X14017658
- 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 angstrom resolution at a synchrotron beamline and belonged to either space group P6(1) or P6(5), with unit-cell parameters a = b = 109.10, c = 238.97 angstrom.
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