Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin-related protein 3.
Myotubularin-related proteins are a large family of phosphatases that have the catalytic activity of dephosphorylating the phospholipid molecules phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. Each of the 14 family members contains a phosphatase catalytic domain, which is inactive in six family members owing to amino-acid changes in a key motif for the activity. All of the members also bear PH-GRAM domains, which have low homologies between them and have roles that are not yet clear. Here, the cloning, expression, purification and crystallization of human myotubularin-related protein 3 encompassing the PH-GRAM and the phosphatase catalytic domain are reported. Preliminary X-ray crystallographic analysis shows that the crystals diffracted to 3.30 Å resolution at a synchrotron X-ray source. The crystals belonged to space group C2, with unit-cell parameters a = 323.3, b = 263.3, c = 149.4 Å, β = 109.7°.
['Son|Ji Young|JY|', 'Lee|Jee Un|JU|', 'Yoo|Ki-Young|KY|', 'Shin|Woori|W|', 'Im|Dong-Won|DW|', 'Kim|Seung Jun|SJ|', 'Ryu|Seong Eon|SE|', 'Heo|Yong-Seok|YS|']
D000595:Amino Acid Sequence D001483:Base Sequence D003460:Crystallization D018360:Crystallography, X-Ray D017931:DNA Primers D006801:Humans D008969:Molecular Sequence Data D011487:Protein Conformation D054558:Protein Tyrosine Phosphatases, Non-Receptor
myotubularin-related proteins phosphatase PH-GRAM domain MTMR3 phosphoinositide