5C16

Myotubularin-related proetin 1

Summary for 5C16

• Entry DOI: 10.2210/pdb5c16/pdb
• Descriptor: Myotubularin-related protein 1, PHOSPHATE ION (3 entities in total)
• Functional Keywords: mtmr, phosphatase, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q13613
• Total number of polymer chains: 4
• Total formula weight: 262182.98

Authors

Lee, B.I.,Bong, S.M. (deposition date: 2015-06-13, release date: 2016-04-27, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.07 Å)