Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4
| Autor: | Jee Un Lee, Seung Jun Kim, Yong-Seok Heo, Dong-Won Im, Ji Young Son, Woori Shin, Seong Eon Ryu, Ki-Young Yoo |
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| Rok vydání: | 2014 |
| Předmět: |
Protein Conformation
Endosome Molecular Sequence Data Phosphatase Biophysics Biology Crystallography X-Ray Biochemistry Dephosphorylation chemistry.chemical_compound Protein structure Structural Biology Genetics Humans Amino Acid Sequence Phosphatidylinositol DNA Primers Base Sequence Effector Autophagy Protein Tyrosine Phosphatases Non-Receptor Condensed Matter Physics Cell biology Pleckstrin homology domain Crystallography chemistry Crystallization Communications Crystallization |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 70:1280-1283 |
| ISSN: | 2053-230X |
| DOI: | 10.1107/s2053230x14017658 |
| Popis: | 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 inEscherichia 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 groupP61orP65, with unit-cell parametersa=b= 109.10,c= 238.97 Å. |
| Databáze: | OpenAIRE |
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