5c16
From Proteopedia
Myotubularin-related proetin 1
Structural highlights
FunctionMTMR1_HUMAN Lipid phosphatase that has high specificity for phosphatidylinositol 3-phosphate and has no activity with phosphatidylinositol (3,5)-bisphosphate.[1] Publication Abstract from PubMedMyotubularin-related protein 1 (MTMR1) is a phosphatase that belongs to the tyrosine/dual-specificity phosphatase superfamily. MTMR1 has been shown to use phosphatidylinositol 3-monophosphate (PI(3)P) and/or phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) as substrates. Here, we determined the crystal structure of human MTMR1. The refined model consists of the Pleckstrin homology (PH)-GRAM and phosphatase (PTP) domains. The overall structure was highly similar to the previously reported MTMR2 structure. Interestingly, two phosphate molecules were coordinated by strictly conserved residues located in the C(X)5R motif of the active site. Additionally, our biochemical studies confirmed the substrate specificity of MTMR1 for PI(3)P and PI(3,5)P2 over other phosphatidylinositol phosphates. Our structural and enzymatic analyses provide insight into the catalytic mechanism and biochemical properties of MTMR1. Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity.,Bong SM, Son KB, Yang SW, Park JW, Cho JW, Kim KT, Kim H, Kim SJ, Kim YJ, Lee BI PLoS One. 2016 Mar 28;11(3):e0152611. doi: 10.1371/journal.pone.0152611., eCollection 2016. PMID:27018598[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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