Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin-related protein 3
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Authors: Son, Ji Young; Lee, Jee Un; Yoo, Ki-Young; Shin, Woori; Im, Dong-Won; Kim, Seung Jun; Ryu, Seong Eon; Heo, Yong-Seok
Abstract
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 angstrom 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 angstrom, beta = 109.7 degrees.
Membrane binding study of myotubularin related protein 3 (MTMR3)
BIOPHYSICAL JOURNAL
Authors: Burian, A; Cho, WH
Abstract