Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin-related protein 3

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Title
Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin-related protein 3
Author(s)
J Y Son; J U Lee; 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. 1240-1243
Publication Year
2014
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 A 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 A, β = 109.7°.
Keyword
MTMR3myotubularin-related proteinsPH-GRAM domainphosphatasephosphoinositide
ISSN
1744-3091
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S2053230X14015714
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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