5C16

Myotubularin-related proetin 1

5C16 の概要

• エントリーDOI: 10.2210/pdb5c16/pdb
• 分子名称: Myotubularin-related protein 1, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: mtmr, phosphatase, hydrolase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q13613
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 262182.98

構造登録者

Lee, B.I.,Bong, S.M. (登録日: 2015-06-13, 公開日: 2016-04-27, 最終更新日: 2024-03-20)

主引用文献

Bong, S.M.,Son, K.B.,Yang, S.W.,Park, J.W.,Cho, J.W.,Kim, K.T.,Kim, H.,Kim, S.J.,Kim, Y.J.,Lee, B.I.
Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate Specificity
Plos One, 11:e0152611-e0152611, 2016

PubMed Abstract: Myotubularin-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.

PubMed: 27018598
DOI: 10.1371/journal.pone.0152611

実験手法

X-RAY DIFFRACTION (2.07 Å)